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Conserved domains on  [gi|1063678458|ref|NP_173599|]
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filament-like protein (DUF869) [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FPP super family cl26552
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
16-292 2.75e-40

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


The actual alignment was detected with superfamily member pfam05911:

Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 157.53  E-value: 2.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  16 KDELVKQHAKVAEDAVAGWEKAENEVVELKQKLEDAADKNIVLEDRVSHLDGALKECVRQLRQFRDEQEKNIQAAVTEST 95
Cdd:pfam05911   1 KDDLVKQHAKVAEEAVSGWEKAEAEALALKQQLESVTLQKLTAEERAAHLDGALKECMQQLRNVKEEQEQKIHDVVLKKT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  96 KELHSANTGLEKRVLELQKE-------------------------------AEA-----------AKSENMMLRREFLTQ 133
Cdd:pfam05911  81 KEWEKIKAELEAKLVETEQEllraaaendalsrslqerenllmklseeksqAEAeiealksrlesCEKEINSLKYELHVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 134 REDLEIVMIERDLSTQAAETASKQHLDIIKKLAKLEAECRKLRIL----------------------------------- 178
Cdd:pfam05911 161 SKELEIRNEEKNMSRRSADAAHKQHLESVKKIAKLEAECQRLRGLvrkklpgpaalaqmklevemlgrdsgetrlrrspv 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 179 ------------------------------------------------------------AKT--------------SSS 184
Cdd:pfam05911 241 knssphlspdpdfsedslqtphkeneflterllameeetkmlkealakrnselqasrnmcAKTasklsqleaqleelNQG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 185 LSSNQSVDSHS-------------DGGRErvEGSCSDSWAsSAFISELDQIKNEKGGNRSLQGTTSSTEIDLMDDFLEME 251
Cdd:pfam05911 321 QVSMELASSQNpasnppsltsmseDGSDD--EVSCAESWA-SALISELEHFKKEKPKTKSSCKSVGNSDLELMDDFLEME 397
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1063678458 252 RLVALPTETQAKNSKDGYELSLMEKLEKIQAEKDDLEREVK 292
Cdd:pfam05911 398 KLACLSNDKPSNGSHSSSKSSNNKKGEESDSEKDSSESTGK 438
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
272-533 1.45e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 1.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  272 SLMEKLEKIQAEKDDLEREVKCCREAEKRLSLEIEAVVGDKMELEDMLKRVEAEKAELKTSFDVLKDKYQESRVCFQEVD 351
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  352 TKLEKLQAEKDELDSEVICCKEAEKRFSLELEAVVGDKIEMEDELEKMEAEKAELKISFDVIKDQYQESRVCFQEVEMKL 431
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  432 EAMKRELKLANESKTQAESRVTRMEAEVRK--ERIVSDGLKEKCETFEEELRREIEEKTMIKREKVEPKIKQEDIATAAG 509
Cdd:TIGR02168  396 ASLNNEIERLEARLERLEDRRERLQQEIEEllKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
                          250       260
                   ....*....|....*....|....
gi 1063678458  510 KFADCQKTIASLGKQLQSLATLEE 533
Cdd:TIGR02168  476 ALDAAERELAQLQARLDSLERLQE 499
 
Name Accession Description Interval E-value
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
16-292 2.75e-40

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 157.53  E-value: 2.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  16 KDELVKQHAKVAEDAVAGWEKAENEVVELKQKLEDAADKNIVLEDRVSHLDGALKECVRQLRQFRDEQEKNIQAAVTEST 95
Cdd:pfam05911   1 KDDLVKQHAKVAEEAVSGWEKAEAEALALKQQLESVTLQKLTAEERAAHLDGALKECMQQLRNVKEEQEQKIHDVVLKKT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  96 KELHSANTGLEKRVLELQKE-------------------------------AEA-----------AKSENMMLRREFLTQ 133
Cdd:pfam05911  81 KEWEKIKAELEAKLVETEQEllraaaendalsrslqerenllmklseeksqAEAeiealksrlesCEKEINSLKYELHVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 134 REDLEIVMIERDLSTQAAETASKQHLDIIKKLAKLEAECRKLRIL----------------------------------- 178
Cdd:pfam05911 161 SKELEIRNEEKNMSRRSADAAHKQHLESVKKIAKLEAECQRLRGLvrkklpgpaalaqmklevemlgrdsgetrlrrspv 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 179 ------------------------------------------------------------AKT--------------SSS 184
Cdd:pfam05911 241 knssphlspdpdfsedslqtphkeneflterllameeetkmlkealakrnselqasrnmcAKTasklsqleaqleelNQG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 185 LSSNQSVDSHS-------------DGGRErvEGSCSDSWAsSAFISELDQIKNEKGGNRSLQGTTSSTEIDLMDDFLEME 251
Cdd:pfam05911 321 QVSMELASSQNpasnppsltsmseDGSDD--EVSCAESWA-SALISELEHFKKEKPKTKSSCKSVGNSDLELMDDFLEME 397
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1063678458 252 RLVALPTETQAKNSKDGYELSLMEKLEKIQAEKDDLEREVK 292
Cdd:pfam05911 398 KLACLSNDKPSNGSHSSSKSSNNKKGEESDSEKDSSESTGK 438
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
272-533 1.45e-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: 54.68  E-value: 1.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  272 SLMEKLEKIQAEKDDLEREVKCCREAEKRLSLEIEAVVGDKMELEDMLKRVEAEKAELKTSFDVLKDKYQESRVCFQEVD 351
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  352 TKLEKLQAEKDELDSEVICCKEAEKRFSLELEAVVGDKIEMEDELEKMEAEKAELKISFDVIKDQYQESRVCFQEVEMKL 431
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  432 EAMKRELKLANESKTQAESRVTRMEAEVRK--ERIVSDGLKEKCETFEEELRREIEEKTMIKREKVEPKIKQEDIATAAG 509
Cdd:TIGR02168  396 ASLNNEIERLEARLERLEDRRERLQQEIEEllKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
                          250       260
                   ....*....|....*....|....
gi 1063678458  510 KFADCQKTIASLGKQLQSLATLEE 533
Cdd:TIGR02168  476 ALDAAERELAQLQARLDSLERLQE 499
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
77-461 5.48e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 5.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458   77 RQFRDEQEKNIqAAVTESTKELHSANTGLEKRVLELQKEAEAAKSENMMLRREFLTQREDLEIVMIERDLSTQAAETASK 156
Cdd:TIGR02168  676 RREIEELEEKI-EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  157 QHLDIIKKLAKLEAECRKLRILAKTSSSLSSNQsvdshsdggRERVEGSCSDSWASSAFISEL-DQIKNEKGGNRSLQGT 235
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEEL---------EAQIEQLKEELKALREALDELrAELTLLNEEAANLRER 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  236 TSSTEIDLMDDFLEMERLValptetqaknskdgyelslmEKLEKIQAEKDDLEREVKCCREAEKRLSLEIEAVVGDKMEL 315
Cdd:TIGR02168  826 LESLERRIAATERRLEDLE--------------------EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  316 EDMLKRVEAEKAELKTSFDVLKDKYQESRVCFQEVDTKLEKLQAEKDELDSEVICCKEA-EKRFSLELEAVVGDKIEMED 394
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIED 965
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063678458  395 ELEKMEAEKAELKISFDVIKDQYQESRVCFQEVEMKLEAMKRELKLANESKTQAESRVTRMEAEVRK 461
Cdd:TIGR02168  966 DEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
220-439 3.44e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.84  E-value: 3.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 220 DQIKNEKGGN-RSLQGTTSSTeIDLMDDFLEMERLValpTETQAKNSKDGYElslmEKLEKIQAEKDDLEREVKccrEAE 298
Cdd:PRK05771   38 EELSNERLRKlRSLLTKLSEA-LDKLRSYLPKLNPL---REEKKKVSVKSLE----ELIKDVEEELEKIEKEIK---ELE 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 299 KRLSleieavvgdkmELEDMLKRVEAEKAELK--TSFDVLKDKYQESRVCFQEVDTkLEKLQAEKDELDSEVICCKEAEK 376
Cdd:PRK05771  107 EEIS-----------ELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYVSVFVGT-VPEDKLEELKLESDVENVEYIST 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063678458 377 RFSLELEAVVGDK---IEMEDELEKMEAEKAEL--KISFDVIKDQYqESRVCfqEVEMKLEAMKRELK 439
Cdd:PRK05771  175 DKGYVYVVVVVLKelsDEVEEELKKLGFERLELeeEGTPSELIREI-KEELE--EIEKERESLLEELK 239
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
279-463 6.12e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 6.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 279 KIQAEKDDLEREVKCCREaeKRLSLEIEAVVGDKMELEDMLKRVEAEKAELKTSFDVLKDKYQESRVCFQEVDTKLEKLQ 358
Cdd:COG1196   217 ELKEELKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 359 AEKDELDSEVICCKEAEKRFSLELEAVVGDKIEMEDELEKMEAEKAELKISFDVIKDQYQESRVCFQEVEMKLEAMKREL 438
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                         170       180
                  ....*....|....*....|....*
gi 1063678458 439 KLANESKTQAESRVTRMEAEVRKER 463
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELA 399
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
22-437 1.24e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  22 QHAKVAEDAVAGWEKAENEVVELKQKLEDaadknivLEDRVSHLdgalkecvRQLRQFRDEQEKNIQAAVTESTKELHSA 101
Cdd:COG4717   122 EKLLQLLPLYQELEALEAELAELPERLEE-------LEERLEEL--------RELEEELEELEAELAELQEELEELLEQL 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 102 NTGLEKRVLELQKEAEAAKSENMMLRREFLTQREDLEIVMIERDLSTQAAETASKQhldiikklAKLEAECRKLRILAkt 181
Cdd:COG4717   187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE--------ERLKEARLLLLIAA-- 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 182 sssLSSNQSVDSHSDGGRERVEGSCSDSWASSAFISELDQIKNEKGGNRSLQGTTSSTEIDLMDDFLEMERLVALPTETQ 261
Cdd:COG4717   257 ---ALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 262 AKNSKDGYELSLMEKLEKIQAEKDDLEREVKCCREAEKRLSLEIEAVVGDKMELEDMLKRVEaEKAELKTSFDVLKDKYQ 341
Cdd:COG4717   334 LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAE-EYQELKEELEELEEQLE 412
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 342 E---------SRVCFQEVDTKLEKLQAEKDELDSEVICCKEAEKRFSLELEAVVGDkiemeDELEKMEAEKAELKISFDV 412
Cdd:COG4717   413 EllgeleellEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED-----GELAELLQELEELKAELRE 487
                         410       420
                  ....*....|....*....|....*
gi 1063678458 413 IKDQYQESRVCFQEVEMKLEAMKRE 437
Cdd:COG4717   488 LAEEWAALKLALELLEEAREEYREE 512
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
278-439 6.00e-03

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 39.45  E-value: 6.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 278 EKIQAEKDDLEREVKCCREAEKRLSleieavvgdkmELEDMLKRVEAEKAELKTSFDVLKDKYQ---ESRVCFQEVDTKL 354
Cdd:pfam06160 270 ERIDQLYDLLEKEVDAKKYVEKNLP-----------EIEDYLEHAEEQNKELKEELERVQQSYTlneNELERVRGLEKQL 338
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 355 EKLQAEKDELDSEViccKEAEKRFSLELEAVvgdkIEMEDELEKMEAEKAELKISFDVIKDQYQESRVCFQEVEMKLEAM 434
Cdd:pfam06160 339 EELEKRYDEIVERL---EEKEVAYSELQEEL----EEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREI 411

                  ....*
gi 1063678458 435 KRELK 439
Cdd:pfam06160 412 KRLVE 416
 
Name Accession Description Interval E-value
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
16-292 2.75e-40

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 157.53  E-value: 2.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  16 KDELVKQHAKVAEDAVAGWEKAENEVVELKQKLEDAADKNIVLEDRVSHLDGALKECVRQLRQFRDEQEKNIQAAVTEST 95
Cdd:pfam05911   1 KDDLVKQHAKVAEEAVSGWEKAEAEALALKQQLESVTLQKLTAEERAAHLDGALKECMQQLRNVKEEQEQKIHDVVLKKT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  96 KELHSANTGLEKRVLELQKE-------------------------------AEA-----------AKSENMMLRREFLTQ 133
Cdd:pfam05911  81 KEWEKIKAELEAKLVETEQEllraaaendalsrslqerenllmklseeksqAEAeiealksrlesCEKEINSLKYELHVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 134 REDLEIVMIERDLSTQAAETASKQHLDIIKKLAKLEAECRKLRIL----------------------------------- 178
Cdd:pfam05911 161 SKELEIRNEEKNMSRRSADAAHKQHLESVKKIAKLEAECQRLRGLvrkklpgpaalaqmklevemlgrdsgetrlrrspv 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 179 ------------------------------------------------------------AKT--------------SSS 184
Cdd:pfam05911 241 knssphlspdpdfsedslqtphkeneflterllameeetkmlkealakrnselqasrnmcAKTasklsqleaqleelNQG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 185 LSSNQSVDSHS-------------DGGRErvEGSCSDSWAsSAFISELDQIKNEKGGNRSLQGTTSSTEIDLMDDFLEME 251
Cdd:pfam05911 321 QVSMELASSQNpasnppsltsmseDGSDD--EVSCAESWA-SALISELEHFKKEKPKTKSSCKSVGNSDLELMDDFLEME 397
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1063678458 252 RLVALPTETQAKNSKDGYELSLMEKLEKIQAEKDDLEREVK 292
Cdd:pfam05911 398 KLACLSNDKPSNGSHSSSKSSNNKKGEESDSEKDSSESTGK 438
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
272-533 1.45e-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: 54.68  E-value: 1.45e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  272 SLMEKLEKIQAEKDDLEREVKCCREAEKRLSLEIEAVVGDKMELEDMLKRVEAEKAELKTSFDVLKDKYQESRVCFQEVD 351
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  352 TKLEKLQAEKDELDSEVICCKEAEKRFSLELEAVVGDKIEMEDELEKMEAEKAELKISFDVIKDQYQESRVCFQEVEMKL 431
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  432 EAMKRELKLANESKTQAESRVTRMEAEVRK--ERIVSDGLKEKCETFEEELRREIEEKTMIKREKVEPKIKQEDIATAAG 509
Cdd:TIGR02168  396 ASLNNEIERLEARLERLEDRRERLQQEIEEllKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
                          250       260
                   ....*....|....*....|....
gi 1063678458  510 KFADCQKTIASLGKQLQSLATLEE 533
Cdd:TIGR02168  476 ALDAAERELAQLQARLDSLERLQE 499
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
273-459 3.69e-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: 53.52  E-value: 3.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  273 LMEKLEKIQAEKDDLEREVKCCREAEKRLSLEIEAVVGDKMELEDMLKRVEAEKAELKTSFDVLKDKYQESRVCFQEVDT 352
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE 824
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  353 KLEKLQAEKDELDSEVICCKEAEKRFSLELEAVVG-------DKIEMEDELEKMEAEKAELKISFDVIKDQYQESRVCFQ 425
Cdd:TIGR02168  825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAeieeleeLIEELESELEALLNERASLEEALALLRSELEELSEELR 904
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1063678458  426 EVEMKLEAMKRELKLANESKTQAESRVTRMEAEV 459
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
7-541 5.92e-07

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 52.81  E-value: 5.92e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458    7 LILEPVMDSKDELVKQH----AKVAEDAVAGWEKAENEVVELKQKLEDAADKNIV-------LEDRVSHLDGALKECVRQ 75
Cdd:pfam15921  260 LLLQQHQDRIEQLISEHeveiTGLTEKASSARSQANSIQSQLEIIQEQARNQNSMymrqlsdLESTVSQLRSELREAKRM 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458   76 LRQFRDEQEKNIQAAVTEST----------KELHSANTGLEKRVLELQKEAEAAKSENMMLRRefLTQRE---DLEIVMI 142
Cdd:pfam15921  340 YEDKIEELEKQLVLANSELTearterdqfsQESGNLDDQLQKLLADLHKREKELSLEKEQNKR--LWDRDtgnSITIDHL 417
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  143 ERDLSTQAAETaskQHLDIIKKLAKLEAECRKLRILAKTSsslssnqsvdshsdGGRERVEGSCSDSWASSAFISELDQI 222
Cdd:pfam15921  418 RRELDDRNMEV---QRLEALLKAMKSECQGQMERQMAAIQ--------------GKNESLEKVSSLTAQLESTKEMLRKV 480
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  223 KNEKGGNRSLQGTTSSTEIDLMDDFLEMERLVAlPTETQAKNSKDGYELSLMEkLEKIQAEKDDLEREVKCCREAEKRLS 302
Cdd:pfam15921  481 VEELTAKKMTLESSERTVSDLTASLQEKERAIE-ATNAEITKLRSRVDLKLQE-LQHLKNEGDHLRNVQTECEALKLQMA 558
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  303 LEIEAVVGDKMELEDMLKRV----------EAEKAELKTSFDVLKDKYQESRVCFQEVDTKLEKLQAEKDELDSEVICCK 372
Cdd:pfam15921  559 EKDKVIEILRQQIENMTQLVgqhgrtagamQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLV 638
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  373 EAEKRFSLELEAVVGDKIEMEDELEKMEAEKAELKISFDVIKDQYQESRvcfQEVEMKLEAMKRELKLANESKTQAESRV 452
Cdd:pfam15921  639 NAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKS---EEMETTTNKLKMQLKSAQSELEQTRNTL 715
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  453 TRMEA--------------EVRKERIVSDGLKEKCETFEEELRREIEEKTMIKREKVEPKIKQEDIATAAGKFADCQKTI 518
Cdd:pfam15921  716 KSMEGsdghamkvamgmqkQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVL 795
                          570       580
                   ....*....|....*....|...
gi 1063678458  519 ASLGKQLQSLATLEEFLIDTASI 541
Cdd:pfam15921  796 RSQERRLKEKVANMEVALDKASL 818
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
249-460 2.23e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.84  E-value: 2.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  249 EMERLVALPTETQAKNSKDGYE--LSLMEKLEKIQAEKDDLEREVKCC----REAEKRLS---LEIEAVVGDKMELEDML 319
Cdd:TIGR02169  266 RLEEIEQLLEELNKKIKDLGEEeqLRVKEKIGELEAEIASLERSIAEKerelEDAEERLAkleAEIDKLLAEIEELEREI 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  320 KRVEAEKAELKTSFDVLKDKYQESRVCFQEVDT-------KLEKLQAEKDELDSEVICCKEAEKRFSLELEAVVGDKIEM 392
Cdd:TIGR02169  346 EEERKRRDKLTEEYAELKEELEDLRAELEEVDKefaetrdELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADL 425
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063678458  393 EDELEKMEAEKAELKISFDVIKDQYQESRVCFQE-------VEMKLEAMKRELKLANESKTQAESRVTRMEAEVR 460
Cdd:TIGR02169  426 NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQlaadlskYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
77-461 5.48e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 5.48e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458   77 RQFRDEQEKNIqAAVTESTKELHSANTGLEKRVLELQKEAEAAKSENMMLRREFLTQREDLEIVMIERDLSTQAAETASK 156
Cdd:TIGR02168  676 RREIEELEEKI-EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  157 QHLDIIKKLAKLEAECRKLRILAKTSSSLSSNQsvdshsdggRERVEGSCSDSWASSAFISEL-DQIKNEKGGNRSLQGT 235
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEEL---------EAQIEQLKEELKALREALDELrAELTLLNEEAANLRER 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  236 TSSTEIDLMDDFLEMERLValptetqaknskdgyelslmEKLEKIQAEKDDLEREVKCCREAEKRLSLEIEAVVGDKMEL 315
Cdd:TIGR02168  826 LESLERRIAATERRLEDLE--------------------EQIEELSEDIESLAAEIEELEELIEELESELEALLNERASL 885
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  316 EDMLKRVEAEKAELKTSFDVLKDKYQESRVCFQEVDTKLEKLQAEKDELDSEVICCKEA-EKRFSLELEAVVGDKIEMED 394
Cdd:TIGR02168  886 EEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIED 965
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063678458  395 ELEKMEAEKAELKISFDVIKDQYQESRVCFQEVEMKLEAMKRELKLANESKTQAESRVTRMEAEVRK 461
Cdd:TIGR02168  966 DEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
220-439 3.44e-05

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 46.84  E-value: 3.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 220 DQIKNEKGGN-RSLQGTTSSTeIDLMDDFLEMERLValpTETQAKNSKDGYElslmEKLEKIQAEKDDLEREVKccrEAE 298
Cdd:PRK05771   38 EELSNERLRKlRSLLTKLSEA-LDKLRSYLPKLNPL---REEKKKVSVKSLE----ELIKDVEEELEKIEKEIK---ELE 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 299 KRLSleieavvgdkmELEDMLKRVEAEKAELK--TSFDVLKDKYQESRVCFQEVDTkLEKLQAEKDELDSEVICCKEAEK 376
Cdd:PRK05771  107 EEIS-----------ELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYVSVFVGT-VPEDKLEELKLESDVENVEYIST 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063678458 377 RFSLELEAVVGDK---IEMEDELEKMEAEKAEL--KISFDVIKDQYqESRVCfqEVEMKLEAMKRELK 439
Cdd:PRK05771  175 DKGYVYVVVVVLKelsDEVEEELKKLGFERLELeeEGTPSELIREI-KEELE--EIEKERESLLEELK 239
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
273-462 3.49e-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: 46.98  E-value: 3.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  273 LMEKLEKIQAEKDDLEREVKCCREAEKRLSLEIEAVVGDKMELEDML-----KRVEAEKAELKTSFDVLKDKYQESRVCF 347
Cdd:TIGR02169  742 LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIEQKL 821
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  348 QEVDTKLEKLQAEKDELDSEVICCKEAEKRFSLELEAVVGDKIEMEDELEK-------MEAEKAELKISFDVIKDQYQES 420
Cdd:TIGR02169  822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEleaalrdLESRLGDLKKERDELEAQLREL 901
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1063678458  421 RVCFQEVEMKLEAMKRELKLANESKTQAESRVTRMEAEVRKE 462
Cdd:TIGR02169  902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
279-463 6.12e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 6.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 279 KIQAEKDDLEREVKCCREaeKRLSLEIEAVVGDKMELEDMLKRVEAEKAELKTSFDVLKDKYQESRVCFQEVDTKLEKLQ 358
Cdd:COG1196   217 ELKEELKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 359 AEKDELDSEVICCKEAEKRFSLELEAVVGDKIEMEDELEKMEAEKAELKISFDVIKDQYQESRVCFQEVEMKLEAMKREL 438
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
                         170       180
                  ....*....|....*....|....*
gi 1063678458 439 KLANESKTQAESRVTRMEAEVRKER 463
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELA 399
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
294-528 1.71e-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: 45.05  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  294 CREAE-KRLSLEIEAVVGDKMELEDMLKRVEAEKAELKTSFDVLKDKYQESRVCFQEVDTKLEKLQAEKDELDSEVICCK 372
Cdd:TIGR02168  674 ERRREiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLS 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  373 EAEKRFSLELEAVVGDKIEMEDELEKMEAEKAELKISFDVIKDQyqesrvcFQEVEMKLEAMKRELKLANESKTQAESRV 452
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE-------LKALREALDELRAELTLLNEEAANLRERL 826
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063678458  453 TRMEAEVRkerivsdglkekcetfeeelrreiEEKTMIKREKVEPKIKQEDIATAAGKFADCQKTIASLGKQLQSL 528
Cdd:TIGR02168  827 ESLERRIA------------------------ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEAL 878
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
273-463 4.51e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.49  E-value: 4.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 273 LMEKLEKIQAEKDDLEREVKCCREAEKRLSLEIEAVVGDkMELEDM-LKRVEAEKAELKTSFDVLKDKYQESRVCFQEVD 351
Cdd:PRK02224  263 LRETIAETEREREELAEEVRDLRERLEELEEERDDLLAE-AGLDDAdAEAVEARREELEDRDEELRDRLEECRVAAQAHN 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 352 TKLEKLQAEKDELDSEVICCKEAEKRFSLELEAVVGDKIEMEDELEKMEAEKAELKISFDVIKDQyqesrvcfqevemkL 431
Cdd:PRK02224  342 EEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD--------------L 407
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1063678458 432 EAMKRELKLANESKTQAESRVTRMEAEVRKER 463
Cdd:PRK02224  408 GNAEDFLEELREERDELREREAELEATLRTAR 439
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
22-437 1.24e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  22 QHAKVAEDAVAGWEKAENEVVELKQKLEDaadknivLEDRVSHLdgalkecvRQLRQFRDEQEKNIQAAVTESTKELHSA 101
Cdd:COG4717   122 EKLLQLLPLYQELEALEAELAELPERLEE-------LEERLEEL--------RELEEELEELEAELAELQEELEELLEQL 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 102 NTGLEKRVLELQKEAEAAKSENMMLRREFLTQREDLEIVMIERDLSTQAAETASKQhldiikklAKLEAECRKLRILAkt 181
Cdd:COG4717   187 SLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE--------ERLKEARLLLLIAA-- 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 182 sssLSSNQSVDSHSDGGRERVEGSCSDSWASSAFISELDQIKNEKGGNRSLQGTTSSTEIDLMDDFLEMERLVALPTETQ 261
Cdd:COG4717   257 ---ALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPD 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 262 AKNSKDGYELSLMEKLEKIQAEKDDLEREVKCCREAEKRLSLEIEAVVGDKMELEDMLKRVEaEKAELKTSFDVLKDKYQ 341
Cdd:COG4717   334 LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAE-EYQELKEELEELEEQLE 412
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 342 E---------SRVCFQEVDTKLEKLQAEKDELDSEVICCKEAEKRFSLELEAVVGDkiemeDELEKMEAEKAELKISFDV 412
Cdd:COG4717   413 EllgeleellEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED-----GELAELLQELEELKAELRE 487
                         410       420
                  ....*....|....*....|....*
gi 1063678458 413 IKDQYQESRVCFQEVEMKLEAMKRE 437
Cdd:COG4717   488 LAEEWAALKLALELLEEAREEYREE 512
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
259-471 2.74e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 259 ETQAKNSKDGYELSLMEKLEKIQAEKDDLEREvkccREAEKRLSLEIEAVVGDKMELEDMLKRVEAEKAELKTSFDVLKD 338
Cdd:COG1196   290 EYELLAELARLEQDIARLEERRRELEERLEEL----EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 339 KYQESRVCFQEVDTKLEKLQAEKDELDSEVICCKEAEKRFSLELEAVVGDKIEMEDELEKMEAEKAELKISFDVIKDQYQ 418
Cdd:COG1196   366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063678458 419 ESRVCFQEVEMKLEAMKRELKLANESKTQAESRVTRMEAEVRKERIVSDGLKE 471
Cdd:COG1196   446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
272-463 3.51e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 272 SLMEKLEKIQAEK-------DDLEREVKCCREAEKRLSLEIEAVVGDKMELEDMLKRVEAEKAELKTSFDVLKDKYQESR 344
Cdd:COG1196   257 ELEAELAELEAELeelrlelEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 345 vcfqevdTKLEKLQAEKDELDSEVICCKEAEKRFSLELEAVVGDKIEMEDELEKMEAEKAELKISFDVIKDQYQESRVCF 424
Cdd:COG1196   337 -------EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1063678458 425 QEVEMKLEAMKRELKLANESKTQAESRVTRMEAEVRKER 463
Cdd:COG1196   410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
272-463 3.67e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 272 SLMEKLEKIQAEKDDLEREVKCCREAEKRLS---LEIEAVVGDKMELEDMLKRVEAEKAELKTSFDVLKDKYQESRVcFQ 348
Cdd:PRK03918  211 EISSELPELREELEKLEKEVKELEELKEEIEeleKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LK 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 349 EVDTKLEKLQAEKDELDSEVICCKEAEKRFSLELEAVvgdkIEMEDELEKMEAEKAELKISFDVIKDQYQESRVCFQEVE 428
Cdd:PRK03918  290 EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGI----EERIKELEEKEERLEELKKKLKELEKRLEELEERHELYE 365
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063678458 429 MKLEAMKRELKLANESKTQAESRVTRMEAEVRKER 463
Cdd:PRK03918  366 EAKAKKEELERLKKRLTGLTPEKLEKELEELEKAK 400
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
275-454 4.08e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 4.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  275 EKLEKIQAEKDDLEREVKCCREAEKRLSLEIEAVVG----------------DKMELEDMLKRVEAEKAELKTSFDVLKd 338
Cdd:COG4913    610 AKLAALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaeyswdeiDVASAEREIAELEAELERLDASSDDLA- 688
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  339 kyqesrvcfqEVDTKLEKLQAEKDELDSEVICCKEAEKRFSLELEAVVGDKIEMEDELEkmEAEKAELKISFDVIKDQYQ 418
Cdd:COG4913    689 ----------ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLE--AAEDLARLELRALLEERFA 756
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1063678458  419 ESRVCFQEVEMKlEAMKRELKLANESKTQAESRVTR 454
Cdd:COG4913    757 AALGDAVERELR-ENLEERIDALRARLNRAEEELER 791
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
275-442 4.54e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.82  E-value: 4.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 275 EKLEKIQAEKDDL----EREVKCCREAEKRLSleieavvgdkmELEDMLKRVEAEKAELKTSFDVLKDKYQ---ESRVCF 347
Cdd:PRK04778  282 EKNEEIQERIDQLydilEREVKARKYVEKNSD-----------TLPDFLEHAKEQNKELKEEIDRVKQSYTlneSELESV 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 348 QEVDTKLEKLQAEKDELDSEViccKEAEKRFSLELEAVvgdkIEMEDELEKMEAEKAELKISFDVIKDQYQESRVCFQEV 427
Cdd:PRK04778  351 RQLEKQLESLEKQYDEITERI---AEQEIAYSELQEEL----EEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERY 423
                         170
                  ....*....|....*
gi 1063678458 428 EMKLEAMKRELKLAN 442
Cdd:PRK04778  424 RNKLHEIKRYLEKSN 438
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
278-439 6.00e-03

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


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 39.45  E-value: 6.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 278 EKIQAEKDDLEREVKCCREAEKRLSleieavvgdkmELEDMLKRVEAEKAELKTSFDVLKDKYQ---ESRVCFQEVDTKL 354
Cdd:pfam06160 270 ERIDQLYDLLEKEVDAKKYVEKNLP-----------EIEDYLEHAEEQNKELKEELERVQQSYTlneNELERVRGLEKQL 338
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 355 EKLQAEKDELDSEViccKEAEKRFSLELEAVvgdkIEMEDELEKMEAEKAELKISFDVIKDQYQESRVCFQEVEMKLEAM 434
Cdd:pfam06160 339 EELEKRYDEIVERL---EEKEVAYSELQEEL----EEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREI 411

                  ....*
gi 1063678458 435 KRELK 439
Cdd:pfam06160 412 KRLVE 416
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
9-406 7.49e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 7.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458   9 LEPVMDSKDELVKQHAKVAEDAVAGWEKAENEVVELKQKLEDAADKNIVLEDRVSHLDGALKECVRQLRQFRDEQEKNIQ 88
Cdd:COG1196   349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458  89 A--AVTESTKELHSANTGLEKRVLELQKEAEAAKSENMMLRREFLTQREDLEIVMIE------RDLSTQAAETASKQHLD 160
Cdd:COG1196   429 AlaELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEElaeaaaRLLLLLEAEADYEGFLE 508
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 161 IIKKLAKLEAECRKLRILAKTSSSLSSNQSVDSHSDGGRERVEGSCSDSWASS------------AFISELDQIKNEKGG 228
Cdd:COG1196   509 GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAaieylkaakagrATFLPLDKIRARAAL 588
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 229 NRSLQGTTSSTEIDLMDD---------FLEMERLVALPTETQAKNSKDGYELSLMEKLEKIQAEKDDLEREVKCCREAEK 299
Cdd:COG1196   589 AAALARGAIGAAVDLVASdlreadaryYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678458 300 RLSLEIEAVVGDKMELEDMLKRVEAEKAELKTSFDVLKDKYQESRVcfQEVDTKLEKLQAEKDELDSEVICCKEAEKRFS 379
Cdd:COG1196   669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE--ERLEEELEEEALEEQLEAEREELLEELLEEEE 746
                         410       420       430
                  ....*....|....*....|....*....|...
gi 1063678458 380 LELEAVVGDKIEMED------ELEKMEAEKAEL 406
Cdd:COG1196   747 LLEEEALEELPEPPDleelerELERLEREIEAL 779
 
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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