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Conserved domains on  [gi|297798414|ref|XP_002867091|]
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uncharacterized protein LOC9305179 isoform X3 [Arabidopsis lyrata subsp. lyrata]

Protein Classification

PEARLI-4 domain-containing protein( domain architecture ID 10526299)

PEARLI-4 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PEARLI-4 pfam05278
Arabidopsis phospholipase-like protein (PEARLI 4); This family contains several ...
163-384 2.15e-110

Arabidopsis phospholipase-like protein (PEARLI 4); This family contains several phospholipase-like proteins from Arabidopsis thaliana which are homologous to PEARLI 4.


:

Pssm-ID: 253129 [Multi-domain]  Cd Length: 234  Bit Score: 322.94  E-value: 2.15e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414  163 GGETRLFSFLSLPRSHEEESNDDYTDDDEENNNEIGVELDLESVMSDTFVSVGKYRVRSGSSTILSAIIEKHGDIAQNCK 242
Cdd:pfam05278   3 KGSVLLFPELSLPPSERKESRDIFSDDDEENNNEEPVELDLQSVMSDSYVSVGKYRVRASVSTTLQAIIDKHGDIASNSK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414  243 LESDSMRSRYLECLCSLMQELRSTPVGQLSKIKVKEMLAVLKDLESVNIEVAWLRSVLEEFAQSL------EDAENEKER 316
Cdd:pfam05278  83 LQSLSTRSYYLECLASVVQELQSTPLRQLSESRVKEMLAVVKDLESVKIRVGWLRSVLEEFAEAVeyfdqqETAVVEKER 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297798414  317 HDGLVKAKKEELEAQETDLVRMEKEVAEARLRIEETRAQMVEIEAERSRLEK----MGFKMEKFKGKSFIDE 384
Cdd:pfam05278 163 HERDVLLKKQEMEKQEAELVRKEKEVKEFREKVEEMAGRLGELEMKRLRLEKrldfLGSKVEKFKGKSFLDE 234
 
Name Accession Description Interval E-value
PEARLI-4 pfam05278
Arabidopsis phospholipase-like protein (PEARLI 4); This family contains several ...
163-384 2.15e-110

Arabidopsis phospholipase-like protein (PEARLI 4); This family contains several phospholipase-like proteins from Arabidopsis thaliana which are homologous to PEARLI 4.


Pssm-ID: 253129 [Multi-domain]  Cd Length: 234  Bit Score: 322.94  E-value: 2.15e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414  163 GGETRLFSFLSLPRSHEEESNDDYTDDDEENNNEIGVELDLESVMSDTFVSVGKYRVRSGSSTILSAIIEKHGDIAQNCK 242
Cdd:pfam05278   3 KGSVLLFPELSLPPSERKESRDIFSDDDEENNNEEPVELDLQSVMSDSYVSVGKYRVRASVSTTLQAIIDKHGDIASNSK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414  243 LESDSMRSRYLECLCSLMQELRSTPVGQLSKIKVKEMLAVLKDLESVNIEVAWLRSVLEEFAQSL------EDAENEKER 316
Cdd:pfam05278  83 LQSLSTRSYYLECLASVVQELQSTPLRQLSESRVKEMLAVVKDLESVKIRVGWLRSVLEEFAEAVeyfdqqETAVVEKER 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297798414  317 HDGLVKAKKEELEAQETDLVRMEKEVAEARLRIEETRAQMVEIEAERSRLEK----MGFKMEKFKGKSFIDE 384
Cdd:pfam05278 163 HERDVLLKKQEMEKQEAELVRKEKEVKEFREKVEEMAGRLGELEMKRLRLEKrldfLGSKVEKFKGKSFLDE 234
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
270-386 3.08e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 3.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414   270 QLSKIKVKEMLAVLKDLESVNIEVAWLRSVLEEFAQSLEDAENEKERHDGLVKAKKEELEAQETDLVRMEKEVA------ 343
Cdd:TIGR02169  280 KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDklteey 359
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 297798414   344 ---EARLRIEETRAQMVEIEAERSRLEKMGFKMEKFKGKSFIDELL 386
Cdd:TIGR02169  360 aelKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
276-363 3.50e-05

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: 44.53  E-value: 3.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414 276 VKEMLAVLKDLESVNIEVAWLRSVLEEFAQSLEDAENEKERHDGLVKAKKEELEAQETDLVRMEKEVAEARLRIEETRAQ 355
Cdd:COG1579    2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81

                 ....*...
gi 297798414 356 MVEIEAER 363
Cdd:COG1579   82 LGNVRNNK 89
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
284-386 2.91e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414 284 KDLESVNIEVAWLRSVLEEFAQSLEDAENEKER---HDGLVKAKKEELEAQETDLVRMEKEVAEARLRIEETRAQMVEIE 360
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
                         90       100
                 ....*....|....*....|....*..
gi 297798414 361 AERSRLEKMGFKMEKF-KGKSFIDELL 386
Cdd:PRK03918 280 EKVKELKELKEKAEEYiKLSEFYEEYL 306
 
Name Accession Description Interval E-value
PEARLI-4 pfam05278
Arabidopsis phospholipase-like protein (PEARLI 4); This family contains several ...
163-384 2.15e-110

Arabidopsis phospholipase-like protein (PEARLI 4); This family contains several phospholipase-like proteins from Arabidopsis thaliana which are homologous to PEARLI 4.


Pssm-ID: 253129 [Multi-domain]  Cd Length: 234  Bit Score: 322.94  E-value: 2.15e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414  163 GGETRLFSFLSLPRSHEEESNDDYTDDDEENNNEIGVELDLESVMSDTFVSVGKYRVRSGSSTILSAIIEKHGDIAQNCK 242
Cdd:pfam05278   3 KGSVLLFPELSLPPSERKESRDIFSDDDEENNNEEPVELDLQSVMSDSYVSVGKYRVRASVSTTLQAIIDKHGDIASNSK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414  243 LESDSMRSRYLECLCSLMQELRSTPVGQLSKIKVKEMLAVLKDLESVNIEVAWLRSVLEEFAQSL------EDAENEKER 316
Cdd:pfam05278  83 LQSLSTRSYYLECLASVVQELQSTPLRQLSESRVKEMLAVVKDLESVKIRVGWLRSVLEEFAEAVeyfdqqETAVVEKER 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 297798414  317 HDGLVKAKKEELEAQETDLVRMEKEVAEARLRIEETRAQMVEIEAERSRLEK----MGFKMEKFKGKSFIDE 384
Cdd:pfam05278 163 HERDVLLKKQEMEKQEAELVRKEKEVKEFREKVEEMAGRLGELEMKRLRLEKrldfLGSKVEKFKGKSFLDE 234
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
270-386 3.08e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 3.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414   270 QLSKIKVKEMLAVLKDLESVNIEVAWLRSVLEEFAQSLEDAENEKERHDGLVKAKKEELEAQETDLVRMEKEVA------ 343
Cdd:TIGR02169  280 KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDklteey 359
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 297798414   344 ---EARLRIEETRAQMVEIEAERSRLEKMGFKMEKFKGKSFIDELL 386
Cdd:TIGR02169  360 aelKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELK 405
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
276-363 3.50e-05

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: 44.53  E-value: 3.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414 276 VKEMLAVLKDLESVNIEVAWLRSVLEEFAQSLEDAENEKERHDGLVKAKKEELEAQETDLVRMEKEVAEARLRIEETRAQ 355
Cdd:COG1579    2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81

                 ....*...
gi 297798414 356 MVEIEAER 363
Cdd:COG1579   82 LGNVRNNK 89
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
284-367 5.18e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 5.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414   284 KDLESVNIEVAWLRSVLEEFAQSLEDAENEKERHDGLVKAKKEELEAQETDLVRMEKEVAEARLRIEETRAQMVEIEAER 363
Cdd:TIGR02168  852 EDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL 931

                   ....
gi 297798414   364 SRLE 367
Cdd:TIGR02168  932 EGLE 935
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
284-368 9.19e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 9.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414 284 KDLESVNIEVAWLRsvLEEFAQSLEDAENEKERHDGLVKAKKEELEAQETDLVRMEKEVAEARLRIEETRAQMVEIEAER 363
Cdd:COG1196  220 EELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                 ....*
gi 297798414 364 SRLEK 368
Cdd:COG1196  298 ARLEQ 302
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
270-368 1.78e-04

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: 42.60  E-value: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414 270 QLSKIK-VKEMLAVLKDLESVNIEvawlRSVLEEfaqSLEDAENEKERHDGLVKAKKEELEAQETDLvrmEKEVAEARLR 348
Cdd:COG1579   81 QLGNVRnNKEYEALQKEIESLKRR----ISDLED---EILELMERIEELEEELAELEAELAELEAEL---EEKKAELDEE 150
                         90       100
                 ....*....|....*....|
gi 297798414 349 IEETRAQMVEIEAERSRLEK 368
Cdd:COG1579  151 LAELEAELEELEAEREELAA 170
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
276-368 2.50e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 2.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414 276 VKEMLAVLKDLESVNIEVAWLRSVLEEFAQSLEDAENEKERHDGLVKAKKEELEAQETDLVRMEKEVAEARLRIEETRAQ 355
Cdd:COG4372   37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116
                         90
                 ....*....|...
gi 297798414 356 MVEIEAERSRLEK 368
Cdd:COG4372  117 LEELQKERQDLEQ 129
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
284-386 2.82e-04

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: 42.44  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414 284 KDLESVNIEVAWLRSVLEEFAQSLEDAENEKERHDGLVKAKKEELEAQETDLVRMEKEVAEARLRIEETRAQmveIEAER 363
Cdd:COG4942   27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE---LEAQK 103
                         90       100
                 ....*....|....*....|...
gi 297798414 364 SRLEKMGFKMEKFKGKSFIDELL 386
Cdd:COG4942  104 EELAELLRALYRLGRQPPLALLL 126
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
272-367 3.71e-04

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: 42.74  E-value: 3.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414   272 SKIKVKEMLAVLKD-LESVNIEVAWLRSVLEEFAQSLEDAENekerhdgLVKAKKEELEAQETDLVRMEKEVAEARLRIE 350
Cdd:TIGR02168  331 KLDELAEELAELEEkLEELKEELESLEAELEELEAELEELES-------RLEELEEQLETLRSKVAQLELQIASLNNEIE 403
                           90
                   ....*....|....*..
gi 297798414   351 ETRAQMVEIEAERSRLE 367
Cdd:TIGR02168  404 RLEARLERLEDRRERLQ 420
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
277-368 2.17e-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: 40.43  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414   277 KEMLAVLKDLESVNIEVAWLRSVLEEFAQSLEDAENEKERHDGLVKAKKEELEAQETDLVRMEKEVAEARLRIEETRAQM 356
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
                           90
                   ....*....|..
gi 297798414   357 VEIEAERSRLEK 368
Cdd:TIGR02168  778 AEAEAEIEELEA 789
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
284-386 2.91e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 2.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414 284 KDLESVNIEVAWLRSVLEEFAQSLEDAENEKER---HDGLVKAKKEELEAQETDLVRMEKEVAEARLRIEETRAQMVEIE 360
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE 279
                         90       100
                 ....*....|....*....|....*..
gi 297798414 361 AERSRLEKMGFKMEKF-KGKSFIDELL 386
Cdd:PRK03918 280 EKVKELKELKEKAEEYiKLSEFYEEYL 306
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
281-368 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: 39.67  E-value: 3.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414   281 AVLKDLESVNIEVAWLRSVLEEFAQSLEDAENEK---ERHDGLVKAKKE--------ELEAQETDLVRMEKEVAEAR--- 346
Cdd:TIGR02169  174 KALEELEEVEENIERLDLIIDEKRQQLERLRRERekaERYQALLKEKREyegyellkEKEALERQKEAIERQLASLEeel 253
                           90       100
                   ....*....|....*....|....*.
gi 297798414   347 ----LRIEETRAQMVEIEAERSRLEK 368
Cdd:TIGR02169  254 ekltEEISELEKRLEEIEQLLEELNK 279
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
275-379 3.71e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 3.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414 275 KVKEMLAVLKDLESVNIEVAWLR----------SVLEEFAQSLEDAENEKERHDGLVKAKK-EELEAQETDLVRMEKEVA 343
Cdd:PRK03918 322 EINGIEERIKELEEKEERLEELKkklkelekrlEELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKE 401
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 297798414 344 EARLRIEETRAQMVEIEAERSRLEKMGFKMEKFKGK 379
Cdd:PRK03918 402 EIEEEISKITARIGELKKEIKELKKAIEELKKAKGK 437
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
300-368 3.86e-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: 38.98  E-value: 3.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297798414 300 LEEFAQSLEDAENEKERHDGLVKAKKEELEAQETDLVRMEKEVAEARLRIEETRAQMVEIEAERSRLEK 368
Cdd:COG4942   22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
PRK14154 PRK14154
heat shock protein GrpE; Provisional
301-386 4.53e-03

heat shock protein GrpE; Provisional


Pssm-ID: 237626 [Multi-domain]  Cd Length: 208  Bit Score: 38.25  E-value: 4.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414 301 EEFAQSLEDAENEKERH-DGLVKAKKEELEAQetdLVRMEKEVAEARLRIEETRAQMVEIeaeRSRLEKMGFKMEKFKGK 379
Cdd:PRK14154  29 EEQEEGGGDGSQEMEPHrEGLEFPSREKLEGQ---LTRMERKVDEYKTQYLRAQAEMDNL---RKRIEREKADIIKFGSK 102

                 ....*..
gi 297798414 380 SFIDELL 386
Cdd:PRK14154 103 QLITDLL 109
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
294-369 4.85e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 4.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414 294 AWLRSVLEEFAQSLEDAENE----KERHDGLvkakkeELEAQETDLVrmeKEVAEARLRIEETRAQMVEIEAERSRLEKM 369
Cdd:COG3206  178 EFLEEQLPELRKELEEAEAAleefRQKNGLV------DLSEEAKLLL---QQLSELESQLAEARAELAEAEARLAALRAQ 248
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
284-385 5.48e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 5.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414 284 KDLESVNIEVAWLRSVLEEFAqSLEDAENEKERHDGLVKAKKEELEAQETDLVRMEKEVAEARLRIEETRAQMVEIEAER 363
Cdd:PRK03918 585 ESVEELEERLKELEPFYNEYL-ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE 663
                         90       100
                 ....*....|....*....|..
gi 297798414 364 SRLEKMGFKMEKFKGKSFIDEL 385
Cdd:PRK03918 664 LREEYLELSRELAGLRAELEEL 685
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
277-385 6.16e-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: 38.90  E-value: 6.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414   277 KEMLAVLKDLESVNIEVAWLRSVLEEFAQSLEDAENEKERHDGLVKAKKEELEAQETDLVRMEKEVAEARLRIEETRAQM 356
Cdd:TIGR02169  688 RELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARI 767
                           90       100
                   ....*....|....*....|....*....
gi 297798414   357 VEIEAERSRLEKMGFKMEKFKGKSFIDEL 385
Cdd:TIGR02169  768 EELEEDLHKLEEALNDLEARLSHSRIPEI 796
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
272-368 7.77e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 7.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297798414 272 SKIKVKEMLAVLKDLESVNIEVAWLRSVLEEFAQSLEDAENEKERHDGLVKAKKEELEAQE--------------TDLVR 337
Cdd:COG1196  220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEleleeaqaeeyellAELAR 299
                         90       100       110
                 ....*....|....*....|....*....|.
gi 297798414 338 MEKEVAEARLRIEETRAQMVEIEAERSRLEK 368
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAELEE 330
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
300-368 9.98e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.99  E-value: 9.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297798414 300 LEEFAQSLEDAENEKERHDGLVKAKKEELEAQETDLVRMEKEVAEARLRIEETRAQMVEIEAERSRLEK 368
Cdd:COG1196  311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
 
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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