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Conserved domains on  [gi|665404360|ref|NP_476916|]
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ninein, isoform H [Drosophila melanogaster]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000037)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
271-740 3.32e-09

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 3.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 271 EEEEVNLQQLTKALEEELRGIDGDHEQSNMLRALAALQATELGNYRLAyRQQHEENLKLRADNKAANQRVALLAVEVDER 350
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE-LAEAEEALLEAEAELAEAEEELEELAEELLE 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 351 HASLEDNSKKQVQQLEQRHASMVREITLRMTNDRDhwtsmtgkLEAQLKSLEQEEIRLRTELELVRTENTELESEQQKAH 430
Cdd:COG1196  391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEE--------LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 431 IQITELLEQNIKLNQELAQTSSSIGGtpehspLRPRRHSEDKEEEMLQLMEKLAALQMENAQLRDKTDELTIEI------ 504
Cdd:COG1196  463 ELLAELLEEAALLEAALAELLEELAE------AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgveaay 536
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 505 --------ESLNVELIRSKTKAKKQEKQEKQEDQESAAT------ATKRRGDSPSKTHLTEESPRLGKQRKCTEGEQSDA 570
Cdd:COG1196  537 eaaleaalAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflpldkIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 571 SNSGDWLALNSELQRSQSQDEELTSLRQRVAELEEELKAAKEGRSLTPESRSKELETSLEQMQRAyedcEDYWQTKLSEE 650
Cdd:COG1196  617 VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL----EELAERLAEEE 692
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 651 RQLFEKERQIYEDEQHESDKKFTELMEKVREYEEQfskDGRLSPIDERDMLEQQYSELEAEAAQLRSSSIQMLEEKAQEI 730
Cdd:COG1196  693 LELEEALLAEEEEERELAEAEEERLEEELEEEALE---EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL 769
                        490
                 ....*....|
gi 665404360 731 SSLQSEIEDL 740
Cdd:COG1196  770 ERLEREIEAL 779
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
271-740 3.32e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 3.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 271 EEEEVNLQQLTKALEEELRGIDGDHEQSNMLRALAALQATELGNYRLAyRQQHEENLKLRADNKAANQRVALLAVEVDER 350
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE-LAEAEEALLEAEAELAEAEEELEELAEELLE 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 351 HASLEDNSKKQVQQLEQRHASMVREITLRMTNDRDhwtsmtgkLEAQLKSLEQEEIRLRTELELVRTENTELESEQQKAH 430
Cdd:COG1196  391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEE--------LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 431 IQITELLEQNIKLNQELAQTSSSIGGtpehspLRPRRHSEDKEEEMLQLMEKLAALQMENAQLRDKTDELTIEI------ 504
Cdd:COG1196  463 ELLAELLEEAALLEAALAELLEELAE------AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgveaay 536
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 505 --------ESLNVELIRSKTKAKKQEKQEKQEDQESAAT------ATKRRGDSPSKTHLTEESPRLGKQRKCTEGEQSDA 570
Cdd:COG1196  537 eaaleaalAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflpldkIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 571 SNSGDWLALNSELQRSQSQDEELTSLRQRVAELEEELKAAKEGRSLTPESRSKELETSLEQMQRAyedcEDYWQTKLSEE 650
Cdd:COG1196  617 VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL----EELAERLAEEE 692
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 651 RQLFEKERQIYEDEQHESDKKFTELMEKVREYEEQfskDGRLSPIDERDMLEQQYSELEAEAAQLRSSSIQMLEEKAQEI 730
Cdd:COG1196  693 LELEEALLAEEEEERELAEAEEERLEEELEEEALE---EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL 769
                        490
                 ....*....|
gi 665404360 731 SSLQSEIEDL 740
Cdd:COG1196  770 ERLEREIEAL 779
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
393-730 8.00e-09

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: 59.30  E-value: 8.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   393 KLEAQLKSLEQEEIRLRTELELVRTENTELESEQQKAHIQITELLEQNIKLNQE---LAQTSSSIGGTPEHSPLRPRRHS 469
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqLEERIAQLSKELTELEAEIEELE 767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   470 EDKEEEMLQLME---KLAALQMENAQLRDKTDELTIEIESLNVELIRSKTKAKKQEKQEKQEDQESAATATkrrgdspSK 546
Cdd:TIGR02168  768 ERLEEAEEELAEaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER-------RL 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   547 THLTEESPRLGKQRKCTEGEQSDASNSGDWL--ALNSELQRSQSQDEELTSLRQRVAELEEELKAAkEGRSLTPESRSKE 624
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELEELIEELesELEALLNERASLEEALALLRSELEELSEELREL-ESKRSELRRELEE 919
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   625 LETSLEQMQRAYEDCE---DYWQTKLSEERQLfekERQIYEDEQHESDKKFTELMEKVREYEEQFSKDGR--LSPIDERD 699
Cdd:TIGR02168  920 LREKLAQLELRLEGLEvriDNLQERLSEEYSL---TLEEAEALENKIEDDEEEARRRLKRLENKIKELGPvnLAAIEEYE 996
                          330       340       350
                   ....*....|....*....|....*....|.
gi 665404360   700 MLEQQYSELEAEAAQLRsSSIQMLEEKAQEI 730
Cdd:TIGR02168  997 ELKERYDFLTAQKEDLT-EAKETLEEAIEEI 1026
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
573-746 2.69e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 2.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 573 SGDWLALNSELQRSQSQDEELTSLRQRVAELEEELKAA-KEGRSLTPESrSKELETSLEQMQRAYEDcedYWQTKLSE-E 650
Cdd:PRK03918 538 KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELlKELEELGFES-VEELEERLKELEPFYNE---YLELKDAEkE 613
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 651 RQLFEKERQIYEDEQHESDKKFTELMEKVREYEEQFSKDGRLSPIDERDMLEQQYSELEAEAAQLRsSSIQMLEEKAQEI 730
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLR-AELEELEKRREEI 692
                        170
                 ....*....|....*.
gi 665404360 731 SSLqseIEDLRQRLGE 746
Cdd:PRK03918 693 KKT---LEKLKEELEE 705
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
548-715 4.10e-03

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: 40.81  E-value: 4.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360  548 HLTEESPRLGKQRKCTEGEQSDASnsgdwlaLNSELQRSQSQDEEltslrQRVAELEEELKAAKEGRSLtpesrskeLET 627
Cdd:pfam05911 685 RLKEEFEQLKSEKENLEVELASCT-------ENLESTKSQLQESE-----QLIAELRSELASLKESNSL--------AET 744
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360  628 SLEQMQRAYEDCE---DYWQTKLSEERQLFEKerqiYEDEQHESDKKFTELMEKVREYEEQF----SKDGRLSPIDERDM 700
Cdd:pfam05911 745 QLKCMAESYEDLEtrlTELEAELNELRQKFEA----LEVELEEEKNCHEELEAKCLELQEQLerneKKESSNCDADQEDK 820
                         170
                  ....*....|....*
gi 665404360  701 LEQQYSELEAEAAQL 715
Cdd:pfam05911 821 KLQQEKEITAASEKL 835
 
Name Accession Description Interval E-value
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
271-740 3.32e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 3.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 271 EEEEVNLQQLTKALEEELRGIDGDHEQSNMLRALAALQATELGNYRLAyRQQHEENLKLRADNKAANQRVALLAVEVDER 350
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE-LAEAEEALLEAEAELAEAEEELEELAEELLE 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 351 HASLEDNSKKQVQQLEQRHASMVREITLRMTNDRDhwtsmtgkLEAQLKSLEQEEIRLRTELELVRTENTELESEQQKAH 430
Cdd:COG1196  391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEE--------LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 431 IQITELLEQNIKLNQELAQTSSSIGGtpehspLRPRRHSEDKEEEMLQLMEKLAALQMENAQLRDKTDELTIEI------ 504
Cdd:COG1196  463 ELLAELLEEAALLEAALAELLEELAE------AAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIgveaay 536
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 505 --------ESLNVELIRSKTKAKKQEKQEKQEDQESAAT------ATKRRGDSPSKTHLTEESPRLGKQRKCTEGEQSDA 570
Cdd:COG1196  537 eaaleaalAAALQNIVVEDDEVAAAAIEYLKAAKAGRATflpldkIRARAALAAALARGAIGAAVDLVASDLREADARYY 616
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 571 SNSGDWLALNSELQRSQSQDEELTSLRQRVAELEEELKAAKEGRSLTPESRSKELETSLEQMQRAyedcEDYWQTKLSEE 650
Cdd:COG1196  617 VLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL----EELAERLAEEE 692
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 651 RQLFEKERQIYEDEQHESDKKFTELMEKVREYEEQfskDGRLSPIDERDMLEQQYSELEAEAAQLRSSSIQMLEEKAQEI 730
Cdd:COG1196  693 LELEEALLAEEEEERELAEAEEERLEEELEEEALE---EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL 769
                        490
                 ....*....|
gi 665404360 731 SSLQSEIEDL 740
Cdd:COG1196  770 ERLEREIEAL 779
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
393-730 8.00e-09

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: 59.30  E-value: 8.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   393 KLEAQLKSLEQEEIRLRTELELVRTENTELESEQQKAHIQITELLEQNIKLNQE---LAQTSSSIGGTPEHSPLRPRRHS 469
Cdd:TIGR02168  688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEveqLEERIAQLSKELTELEAEIEELE 767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   470 EDKEEEMLQLME---KLAALQMENAQLRDKTDELTIEIESLNVELIRSKTKAKKQEKQEKQEDQESAATATkrrgdspSK 546
Cdd:TIGR02168  768 ERLEEAEEELAEaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER-------RL 840
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   547 THLTEESPRLGKQRKCTEGEQSDASNSGDWL--ALNSELQRSQSQDEELTSLRQRVAELEEELKAAkEGRSLTPESRSKE 624
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELEELIEELesELEALLNERASLEEALALLRSELEELSEELREL-ESKRSELRRELEE 919
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   625 LETSLEQMQRAYEDCE---DYWQTKLSEERQLfekERQIYEDEQHESDKKFTELMEKVREYEEQFSKDGR--LSPIDERD 699
Cdd:TIGR02168  920 LREKLAQLELRLEGLEvriDNLQERLSEEYSL---TLEEAEALENKIEDDEEEARRRLKRLENKIKELGPvnLAAIEEYE 996
                          330       340       350
                   ....*....|....*....|....*....|.
gi 665404360   700 MLEQQYSELEAEAAQLRsSSIQMLEEKAQEI 730
Cdd:TIGR02168  997 ELKERYDFLTAQKEDLT-EAKETLEEAIEEI 1026
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
458-740 2.66e-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: 57.76  E-value: 2.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   458 PEHSPLRPRRHSEDKEEEMLQLMEKLAALQMENAQLRDKTDELTIEIESLNVELIRSKTKAKKQEKQEKQEDQESAATAT 537
Cdd:TIGR02168  668 TNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEE 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   538 KRRGDSPSKTHLTEEspRLGKQRKCTEGEQSDASNSGDWLALNSELQRSQSQ----DEELTSLRQRVAELEEEL------ 607
Cdd:TIGR02168  748 RIAQLSKELTELEAE--IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEElkalREALDELRAELTLLNEEAanlrer 825
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   608 -------KAAKEGRSLTPESRSKELETSLEQMQRAYEDCEDYwQTKLSEERQLFEKERQIYEDEQHESDKKFTELMEKVR 680
Cdd:TIGR02168  826 leslerrIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL-IEELESELEALLNERASLEEALALLRSELEELSEELR 904
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   681 EYEEQFSK--------DGRLSPIDER--------DMLEQQYSE---LEAEAAQLRSSSIQMLEEKAQ-EISSLQSEIEDL 740
Cdd:TIGR02168  905 ELESKRSElrreleelREKLAQLELRleglevriDNLQERLSEeysLTLEEAEALENKIEDDEEEARrRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
282-743 3.48e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.17  E-value: 3.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 282 KALEEELRGIDGDHEQSNMLRALAALQATELGNYRLAYRQQHEEnlkLRADNKAANQRVALLAVEVdERHASLEDNSKKQ 361
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE---LELELEEAQAEEYELLAEL-ARLEQDIARLEER 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 362 VQQLEQRHAsmvreitlRMTNDRDHWTSMTGKLEAQLKSLEQEEIRLRTELELVRTENTELESEQQKAHIQITELLEQNI 441
Cdd:COG1196  311 RRELEERLE--------ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 442 KLNQELAQTSSSIGGTpEHSPLRPRRHSEDKEEEMLQLMEKLAALQMENAQLRDKTDELTIEIESLNVELIRSKTKAKKQ 521
Cdd:COG1196  383 ELAEELLEALRAAAEL-AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 522 EKQEKQEDQESAATATKRRGDSPSKTHLTEESPRLGKQRKCTEGEQSD-------ASNSGDWLALNSELQRSQSQDEEL- 593
Cdd:COG1196  462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvkaalllAGLRGLAGAVAVLIGVEAAYEAALe 541
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 594 -----------TSLRQRVAELEEELKAAKEGR----SLTPESRSKELETSLEQMQRAYE----DCEDYWQTKLSEERQLF 654
Cdd:COG1196  542 aalaaalqnivVEDDEVAAAAIEYLKAAKAGRatflPLDKIRARAALAAALARGAIGAAvdlvASDLREADARYYVLGDT 621
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 655 EKERQIYEDEQHESDKKFTELMEKVREyEEQFSKDGRLSPIDERDMLEQQYSELEAEAAQLRSSSIQMLEEKAQEISSLQ 734
Cdd:COG1196  622 LLGRTLVAARLEAALRRAVTLAGRLRE-VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700

                 ....*....
gi 665404360 735 SEIEDLRQR 743
Cdd:COG1196  701 AEEEEEREL 709
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
578-754 6.33e-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: 53.14  E-value: 6.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   578 ALNSELQRSQSQDEEL----TSLRQRVAELEEELKAAKEGRSlTPESRSKELETSLEQMQRAYEdcedywqtKLSEERQL 653
Cdd:TIGR02168  257 ELTAELQELEEKLEELrlevSELEEEIEELQKELYALANEIS-RLEQQKQILRERLANLERQLE--------ELEAQLEE 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   654 FEKERQIYEDEQHESDKKFTELMEKVREYEEQFSKDGRlspidERDMLEQQYSELEAEAAQLRSSSIQMLEEKAQ---EI 730
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLEAELEELEA-----ELEELESRLEELEEQLETLRSKVAQLELQIASlnnEI 402
                          170       180
                   ....*....|....*....|....
gi 665404360   731 SSLQSEIEDLRQRLGESVEILTGA 754
Cdd:TIGR02168  403 ERLEARLERLEDRRERLQQEIEEL 426
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
392-749 2.66e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 2.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   392 GKLEAQLKSLEQEEirLRTELELVRTENTELESEQQKAHIQITELLEQNIKLNQELAQTSSSIggtpehsplrprrhSED 471
Cdd:TIGR02169  221 REYEGYELLKEKEA--LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI--------------KDL 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   472 KEEEMLQLMEKLAALQMENAQLRDKTDELTIEIESLNVEliRSKTKAKKQEKQEKQEDQESAATATKRRgdspsKTHLTE 551
Cdd:TIGR02169  285 GEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEER--LAKLEAEIDKLLAEIEELEREIEEERKR-----RDKLTE 357
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   552 ESprlgkqrkctegeqsdasnsgdwlalnselqrsQSQDEELTSLRQRVAELEEELKAAKEgrsltpesRSKELETSLEQ 631
Cdd:TIGR02169  358 EY---------------------------------AELKEELEDLRAELEEVDKEFAETRD--------ELKDYREKLEK 396
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   632 MQRAYEDCEDYWQTKLSEERQLFEKERQIY------EDEQHESDKKFTELMEKVREYEEQFSkdgrlSPIDERDMLEQQY 705
Cdd:TIGR02169  397 LKREINELKRELDRLQEELQRLSEELADLNaaiagiEAKINELEEEKEDKALEIKKQEWKLE-----QLAADLSKYEQEL 471
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....
gi 665404360   706 SELEAEAAQLRSssiqmleekaqEISSLQSEIEDLRQRLGESVE 749
Cdd:TIGR02169  472 YDLKEEYDRVEK-----------ELSKLQRELAEAEAQARASEE 504
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
394-746 7.58e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 7.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 394 LEAQLKSLEQEEIRLRTELELvRTENTELESEQQKAHIQitelleqniKLNQELAQTSSSIggtpehsplrprrhsEDKE 473
Cdd:COG1196  198 LERQLEPLERQAEKAERYREL-KEELKELEAELLLLKLR---------ELEAELEELEAEL---------------EELE 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 474 EEMLQLMEKLAALQMENAQLRDKTDELTIEIESLNVELIRSKTKAKKQEKqekqedqesaatatkrrgdspSKTHLTEES 553
Cdd:COG1196  253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ---------------------DIARLEERR 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 554 PRLGKQRkctegEQSDAsnsgdwlALNSELQRSQSQDEELTSLRQRVAELEEELKAAKEGRSLTPESRSKELETSLEQMQ 633
Cdd:COG1196  312 RELEERL-----EELEE-------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 634 RAYEDcedyWQTKLSEERQLFEKERQIYEDEQHESDKKFTELMEKVREYEEQFSKDGRLSPIDERDMLEQQYSELEAEAA 713
Cdd:COG1196  380 ELEEL----AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
                        330       340       350
                 ....*....|....*....|....*....|...
gi 665404360 714 QLRSSSIQMLEEKAQEISSLQSEIEDLRQRLGE 746
Cdd:COG1196  456 EEEEALLELLAELLEEAALLEAALAELLEELAE 488
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
319-691 1.30e-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: 48.90  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   319 YRQQHEENLKLRADNKAANQRVALLAVEVDERHASLEDNSKKQVQQLEQRHAsmVREITLRMTNDRdhWTSMTGKLEA-- 396
Cdd:TIGR02168  170 YKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAE--LRELELALLVLR--LEELREELEElq 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   397 -QLKSLEQEEIRLRTELELVRTENTELESEQQKAHIQITELLEQNIKLNQELAQTSSSIGGTPEhSPLRPRRHSEDKEEE 475
Cdd:TIGR02168  246 eELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE-RLANLERQLEELEAQ 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   476 MLQLMEKLAALQMENAQLRDKTDELTIEIESLNVELIRSKTKAKKqekqekqedqesaatatkrrgdspSKTHLTEESPR 555
Cdd:TIGR02168  325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE------------------------LESRLEELEEQ 380
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   556 LGKQRKctegEQSDASNSGDwlALNSELQRSQSQDEELTSLRQR-VAELEEELKAAKEGRSLTPESRSKELETSLEQMQR 634
Cdd:TIGR02168  381 LETLRS----KVAQLELQIA--SLNNEIERLEARLERLEDRRERlQQEIEELLKKLEEAELKELQAELEELEEELEELQE 454
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 665404360   635 AYEDCEDYWQTKLSEERQLFEKERQIYEDEQHESDKKftELMEKVREYEEQFSKDGR 691
Cdd:TIGR02168  455 ELERLEEALEELREELEEAEQALDAAERELAQLQARL--DSLERLQENLEGFSEGVK 509
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
588-699 1.93e-05

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 48.15  E-value: 1.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 588 SQDEELTSLRQRVAELEEELKAAKEGRSLTPESRSKELETSLEQMQRAYEDCEDYWQtklsEERQLFEKERQIYEdEQHE 667
Cdd:COG0542  408 SKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWE----AEKELIEEIQELKE-ELEQ 482
                         90       100       110
                 ....*....|....*....|....*....|....
gi 665404360 668 SDKKFTELMEKVREYEEQFSKDGRLSP--IDERD 699
Cdd:COG0542  483 RYGKIPELEKELAELEEELAELAPLLReeVTEED 516
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
578-771 5.14e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 5.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 578 ALNSELQRSQSQDEELTSLRQRVAELEEELKAAKEGRSLTpESRSKELETSLEQMQRAYEDCEdywQTKLSEERQLFEKE 657
Cdd:COG1196  303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEEL-EEELEEAEEELEEAEAELAEAE---EALLEAEAELAEAE 378
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 658 RQIYEDEQHESDKKFTELMEKVREYEEQFSKDGRLspiDERDMLEQQYSELEAEAAQLRSSSIQmLEEKAQEISSLQSEI 737
Cdd:COG1196  379 EELEELAEELLEALRAAAELAAQLEELEEAEEALL---ERLERLEEELEELEEALAELEEEEEE-EEEALEEAAEEEAEL 454
                        170       180       190
                 ....*....|....*....|....*....|....
gi 665404360 738 EDLRQRLGESVEILTGACELTSESVAQLSAEAGK 771
Cdd:COG1196  455 EEEEEALLELLAELLEEAALLEAALAELLEELAE 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
317-637 8.07e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 8.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 317 LAYRQQHEENLKLRADNKAANQRVALLAVEVDERHASLEDNsKKQVQQLEQRhasmvreitlrmtndrdhwtsmtgkLEA 396
Cdd:COG1196  232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL-RLELEELELE-------------------------LEE 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 397 QLKS---LEQEEIRLRTELELVRTENTELESEQQKAHIQITELLEQNIKLNQELAQTSSSIggtpehsplrprrhsEDKE 473
Cdd:COG1196  286 AQAEeyeLLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL---------------EEAE 350
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 474 EEMLQLMEKLAALQMENAQLRDKTDELTIEIESLNVELIRSKTKAKKQEKQEKQEDQESAATATKRRgdspskTHLTEES 553
Cdd:COG1196  351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE------RLEEELE 424
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 554 PRLGKQRKCTEGEQSDAsnsgdwLALNSELQRSQSQDEELTSLRQRVAELEEELKAAKEGRS--LTPESRSKELETSLEQ 631
Cdd:COG1196  425 ELEEALAELEEEEEEEE------EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAelLEELAEAAARLLLLLE 498

                 ....*.
gi 665404360 632 MQRAYE 637
Cdd:COG1196  499 AEADYE 504
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
334-746 2.45e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 2.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 334 KAANQRVALLAVEVDERHASLEdnskkQVQQLEQRHASMVREITlRMTNDRDHWtsmtgKLEAQLKSLEQEEIRLRTELE 413
Cdd:COG4717   74 KELEEELKEAEEKEEEYAELQE-----ELEELEEELEELEAELE-ELREELEKL-----EKLLQLLPLYQELEALEAELA 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 414 LVRTENTELESEQQkahiQITELLEQNIKLNQELAQTSSSIGgtpehspLRPRRHSEDKEEEMLQLMEKLAALQMENAQL 493
Cdd:COG4717  143 ELPERLEELEERLE----ELRELEEELEELEAELAELQEELE-------ELLEQLSLATEEELQDLAEELEELQQRLAEL 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 494 RDKTDELTIEIESLNVELIRSKTKAKKQEKQEK-QEDQESAATATKRRGDSPSKTHLTEESPRLGKQRKCTEGEQSDAsn 572
Cdd:COG4717  212 EEELEEAQEELEELEEELEQLENELEAAALEERlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALL-- 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 573 sgdWLALNSELQRSQSQDEELTSLRQRVAELEEELKAAKEGRSLTPESRSKELETSLEQMQRAYEDCEDYWQTKLSEERQ 652
Cdd:COG4717  290 ---FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 653 LFEKER-QIYEDEQHESDKKFTELMEKVREYEEqfsKDGRLSPIDERdmLEQQYSELEAEAAQLRSSSI-QMLEEKAQEI 730
Cdd:COG4717  367 ELEQEIaALLAEAGVEDEEELRAALEQAEEYQE---LKEELEELEEQ--LEELLGELEELLEALDEEELeEELEELEEEL 441
                        410
                 ....*....|....*.
gi 665404360 731 SSLQSEIEDLRQRLGE 746
Cdd:COG4717  442 EELEEELEELREELAE 457
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
573-746 2.69e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 2.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 573 SGDWLALNSELQRSQSQDEELTSLRQRVAELEEELKAA-KEGRSLTPESrSKELETSLEQMQRAYEDcedYWQTKLSE-E 650
Cdd:PRK03918 538 KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELlKELEELGFES-VEELEERLKELEPFYNE---YLELKDAEkE 613
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 651 RQLFEKERQIYEDEQHESDKKFTELMEKVREYEEQFSKDGRLSPIDERDMLEQQYSELEAEAAQLRsSSIQMLEEKAQEI 730
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLR-AELEELEKRREEI 692
                        170
                 ....*....|....*.
gi 665404360 731 SSLqseIEDLRQRLGE 746
Cdd:PRK03918 693 KKT---LEKLKEELEE 705
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
558-746 2.77e-04

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: 44.67  E-value: 2.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   558 KQRKCTEGEQSDASNSGDWLALNSELQRSQsqdEELTSLRQRVAELEEELKAAKEGRSlTPESRSKELETSLEQMQRAYE 637
Cdd:TIGR02169  707 LSQELSDASRKIGEIEKEIEQLEQEEEKLK---ERLEELEEDLSSLEQEIENVKSELK-ELEARIEELEEDLHKLEEALN 782
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   638 DCEDywqtKLSEER-QLFEKERQIYEDEQHESDKKFTELMEKV--REYEEQFSKDGRLSPIDERDMLEQQYSELEAEAAQ 714
Cdd:TIGR02169  783 DLEA----RLSHSRiPEIQAELSKLEEEVSRIEARLREIEQKLnrLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
                          170       180       190
                   ....*....|....*....|....*....|..
gi 665404360   715 LRSSsiqmLEEKAQEISSLQSEIEDLRQRLGE 746
Cdd:TIGR02169  859 LNGK----KEELEEELEELEAALRDLESRLGD 886
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
587-769 2.97e-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: 44.66  E-value: 2.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   587 QSQDEELTSLRQRVAELEEELKAAK--------------------EGRSLTPESRSKELETSLEQMQRAYEDCEDYWQtK 646
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEkalaelrkeleeleeeleqlRKELEELSRQISALRKDLARLEAEVEQLEERIA-Q 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   647 LSEERQLFEKERQIYEDEQHESDKKFTELMEKVREYEEQFSKD-GRLSPIDER-DMLEQQYSELEAEAAQLRSSsiqmLE 724
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLkEELKALREAlDELRAELTLLNEEAANLRER----LE 827
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 665404360   725 EKAQEISSLQSEIEDLRQRLG---ESVEILTGACELTSESVAQLSAEA 769
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEelsEDIESLAAEIEELEELIEELESEL 875
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
591-743 4.31e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 4.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360  591 EELTSLRQRVAELEEELKAAKEGRSLTpESRSKELETSLEQMQRAYedcedyWQTKLSEERQLfekERQIyedEQHESDK 670
Cdd:COG4913   288 RRLELLEAELEELRAELARLEAELERL-EARLDALREELDELEAQI------RGNGGDRLEQL---EREI---ERLEREL 354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360  671 KftELMEKVREYEEQFSKDGRLSPIDERDMLEQQ---------YSELEAEAAQLRSSSIQMLEEKAQEISSLQSEIEDLR 741
Cdd:COG4913   355 E--ERERRRARLEALLAALGLPLPASAEEFAALRaeaaalleaLEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432

                  ..
gi 665404360  742 QR 743
Cdd:COG4913   433 RR 434
PRK12704 PRK12704
phosphodiesterase; Provisional
619-772 1.18e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 619 ESRSKELETSLEQM-QRAYEDCEDYWQTKLSEERQLFEKERQIYEDEQHESDKKFTELMEKVREYEEQFSKdgrlspidE 697
Cdd:PRK12704  30 EAKIKEAEEEAKRIlEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR--------K 101
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 665404360 698 RDMLEQQYSELEAEAAQlrsssiqmLEEKAQEISSLQSEIEDLRQrlgESVEILtgaceltsESVAQLSAEAGKS 772
Cdd:PRK12704 102 LELLEKREEELEKKEKE--------LEQKQQELEKKEEELEELIE---EQLQEL--------ERISGLTAEEAKE 157
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
321-668 1.19e-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: 42.75  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   321 QQHEENLKLRADNKAANQRVALLAvEVDERHASLEDnSKKQVQQLEQRHASMVREITLRMTNDRDHWTSMTGKLEAQLKS 400
Cdd:TIGR02169  221 REYEGYELLKEKEALERQKEAIER-QLASLEEELEK-LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGE 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   401 LEQEEIRLRTELELVRTENTELESEQQKAHIQITELLEQNIKLNQELAQtsssiggtpehspLRPRRHS-----EDKEEE 475
Cdd:TIGR02169  299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEE-------------ERKRRDKlteeyAELKEE 365
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   476 MLQLMEKLAALQMENAQLRDKTDELTIEIESLNVELIRSKTkakkqekqekqedqesaatatkrrgdspskthlteESPR 555
Cdd:TIGR02169  366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR-----------------------------------ELDR 410
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   556 LGKQRKCTEGEQSDASNsgdwlALNSELQRSQSQDEELTSLRQRVAELEEELKAAKEGRSltpesrskELETSLEQMQRA 635
Cdd:TIGR02169  411 LQEELQRLSEELADLNA-----AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLS--------KYEQELYDLKEE 477
                          330       340       350
                   ....*....|....*....|....*....|...
gi 665404360   636 YEDCEDYwQTKLSEERQLFEKERQIYEDEQHES 668
Cdd:TIGR02169  478 YDRVEKE-LSKLQRELAEAEAQARASEERVRGG 509
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
393-740 1.21e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.31  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360  393 KLEAQLKSLEQEEIRLRTELELVRTENTELESEQQKAHIQITELLEQNIKLNQELAQTSSSIGGTpehsplrpRRHSEDK 472
Cdd:TIGR04523 215 SLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQN--------NKKIKEL 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360  473 EEEMLQLMEKLAALQMENAQlrDKTDELTIEIESLNVELIRSKTKakkqekqekQEDQESAATATKRRGDSPSKTHLTEE 552
Cdd:TIGR04523 287 EKQLNQLKSEISDLNNQKEQ--DWNKELKSELKNQEKKLEEIQNQ---------ISQNNKIISQLNEQISQLKKELTNSE 355
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360  553 SPRLGKQRKCTEGEQsdasnsgdwlALNSELQRSQSQDEELTSLRQRVAELEEELKAAKEgrsltpesRSKELETSLEQM 632
Cdd:TIGR04523 356 SENSEKQRELEEKQN----------EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK--------LNQQKDEQIKKL 417
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360  633 QRAYEDCEDYwQTKLSEERQLFEKERQIYEDEQHESDKKFTELmEKVREYEEQFSKDGRLSPIDERDMLEQQYSELEAEA 712
Cdd:TIGR04523 418 QQEKELLEKE-IERLKETIIKNNSEIKDLTNQDSVKELIIKNL-DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKE 495
                         330       340       350
                  ....*....|....*....|....*....|....
gi 665404360  713 AQLRS--SSIQMLEEK----AQEISSLQSEIEDL 740
Cdd:TIGR04523 496 KELKKlnEEKKELEEKvkdlTKKISSLKEKIEKL 529
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
596-769 1.30e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 596 LRQRVAELEEELKAAKEGRSLTPESRSKELETSLEQMQRAYEDCEDYWQT---------KLSEERQLFEKERQIYEDEQH 666
Cdd:COG1196  198 LERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAEleeleaeleELEAELAELEAELEELRLELE 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 667 ESDKKFTELMEKVREYEEQFSK-DGRLSPIDERDM-LEQQYSELEAEAAQLRSSSIQM---LEEKAQEISSLQSEIEDLR 741
Cdd:COG1196  278 ELELELEEAQAEEYELLAELARlEQDIARLEERRReLEERLEELEEELAELEEELEELeeeLEELEEELEEAEEELEEAE 357
                        170       180
                 ....*....|....*....|....*...
gi 665404360 742 QRLGESVEILTGACELTSESVAQLSAEA 769
Cdd:COG1196  358 AELAEAEEALLEAEAELAEAEEELEELA 385
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
303-513 1.77e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 41.96  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360  303 ALAALQATELGNyrlayrQQHEENLKLRADNKAANQRVALLAVE-----VDERHASLEdnSKKQVQQLEQRHASMVREIT 377
Cdd:PRK10929   14 SWGAYAATAPDE------KQITQELEQAKAAKTPAQAEIVEALQsalnwLEERKGSLE--RAKQYQQVIDNFPKLSAELR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360  378 LRMTNDRDHWTSMTGKLEAQlkSLEQEEIRLRTEL-ELVRtentELESEQQKAhIQITELL----EQNIKLNQELAQTSS 452
Cdd:PRK10929   86 QQLNNERDEPRSVPPNMSTD--ALEQEILQVSSQLlEKSR----QAQQEQDRA-REISDSLsqlpQQQTEARRQLNEIER 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665404360  453 SIGGTPehSPLRPRRHSedkeeemlqlmeKLAALQMENAQLRDKTDELTIEIESLN--VELIR 513
Cdd:PRK10929  159 RLQTLG--TPNTPLAQA------------QLTALQAESAALKALVDELELAQLSANnrQELAR 207
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
587-776 2.80e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.07  E-value: 2.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 587 QSQDEELTSLRQRVAELEEELKAAKEGRSlTPESRSKELE--TSLEqmqrayEDCEDYWQTKLSEeRQLFEKERQIYEDE 664
Cdd:PRK05771  89 KDVEEELEKIEKEIKELEEEISELENEIK-ELEQEIERLEpwGNFD------LDLSLLLGFKYVS-VFVGTVPEDKLEEL 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 665 QHESDKKFTELMEKVREYeeqfskdGRLSPIDERDMLEQQYSEL---EAEAAQLRSSSI--QMLEEKAQEISSLQSEIED 739
Cdd:PRK05771 161 KLESDVENVEYISTDKGY-------VYVVVVVLKELSDEVEEELkklGFERLELEEEGTpsELIREIKEELEEIEKERES 233
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 665404360 740 LRQRLGESVEILTgacELTSESVAQLSAEAGKSPASS 776
Cdd:PRK05771 234 LLEELKELAKKYL---EELLALYEYLEIELERAEALS 267
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
587-748 3.24e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 3.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 587 QSQDEELTSLRQRVAELEEELKAAKEGRSLTpESRSKELETSLEQMQRAYEDCE----------DYWQTKLSE-----ER 651
Cdd:COG1579   13 QELDSELDRLEHRLKELPAELAELEDELAAL-EARLEAAKTELEDLEKEIKRLEleieeveariKKYEEQLGNvrnnkEY 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 652 QLFEKERQIYEDEQHESDKKFTELMEKVREYEEQFSKdgrlspiderdmLEQQYSELEAEAAQLRSSSIQMLEEKAQEIS 731
Cdd:COG1579   92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAE------------LEAELAELEAELEEKKAELDEELAELEAELE 159
                        170
                 ....*....|....*..
gi 665404360 732 SLQSEIEDLRQRLGESV 748
Cdd:COG1579  160 ELEAEREELAAKIPPEL 176
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
265-507 3.58e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360  265 HVLGFDeeeevNLQQLtKALEEELRGIDGDHEQSNMLRALAALQATELGNYRLAYrQQHEENLKLRADNKAANQRVAlla 344
Cdd:COG4913   602 YVLGFD-----NRAKL-AALEAELAELEEELAEAEERLEALEAELDALQERREAL-QRLAEYSWDEIDVASAEREIA--- 671
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360  345 vEVDERHASLEDNSkkqvQQLEQrhasmvreitlrmtndrdhwtsmtgkLEAQLKSLEQEEIRLRTELELVRTENTELES 424
Cdd:COG4913   672 -ELEAELERLDASS----DDLAA--------------------------LEEQLEELEAELEELEEELDELKGEIGRLEK 720
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360  425 EQQKAhiqitellEQNIKLNQELAQTSSSIGGTPEHSPLRPRRHSEDKEEEMLQLMEKLAAlqmENAQLRDKTDELTIEI 504
Cdd:COG4913   721 ELEQA--------EEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE---RIDALRARLNRAEEEL 789

                  ...
gi 665404360  505 ESL 507
Cdd:COG4913   790 ERA 792
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
548-715 4.10e-03

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: 40.81  E-value: 4.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360  548 HLTEESPRLGKQRKCTEGEQSDASnsgdwlaLNSELQRSQSQDEEltslrQRVAELEEELKAAKEGRSLtpesrskeLET 627
Cdd:pfam05911 685 RLKEEFEQLKSEKENLEVELASCT-------ENLESTKSQLQESE-----QLIAELRSELASLKESNSL--------AET 744
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360  628 SLEQMQRAYEDCE---DYWQTKLSEERQLFEKerqiYEDEQHESDKKFTELMEKVREYEEQF----SKDGRLSPIDERDM 700
Cdd:pfam05911 745 QLKCMAESYEDLEtrlTELEAELNELRQKFEA----LEVELEEEKNCHEELEAKCLELQEQLerneKKESSNCDADQEDK 820
                         170
                  ....*....|....*
gi 665404360  701 LEQQYSELEAEAAQL 715
Cdd:pfam05911 821 KLQQEKEITAASEKL 835
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
587-749 4.42e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 4.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 587 QSQDEELTSLRQRVAELEEELKAAKEgrsltpesRSKELETSLEQMQRAYEDcedywqTKLSEERQLFEKERQIYEDEQH 666
Cdd:COG3206  164 QNLELRREEARKALEFLEEQLPELRK--------ELEEAEAALEEFRQKNGL------VDLSEEAKLLLQQLSELESQLA 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 667 ESDKKFTELMEKVREYEEQFSKDGRLSPIDERD----MLEQQYSELEAEAAQLRSSsiqmLEEKAQEISSLQSEIEDLRQ 742
Cdd:COG3206  230 EARAELAEAEARLAALRAQLGSGPDALPELLQSpviqQLRAQLAELEAELAELSAR----YTPNHPDVIALRAQIAALRA 305

                 ....*..
gi 665404360 743 RLGESVE 749
Cdd:COG3206  306 QLQQEAQ 312
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
572-751 4.69e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 4.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 572 NSGDWLALNSELQRSQSQDEELTSLRQRVAELEEELKAAkegrsltpESRSKELETSLEQMQRAyEDCEDYWQTKLSEER 651
Cdd:COG4717   69 NLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL--------EAELEELREELEKLEKL-LQLLPLYQELEALEA 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 652 QLFEKERQIyedeqhesdkkfTELMEKVREYEEqfskdgrlspiderdmLEQQYSELEAEAAQLRSSSIQMLE----EKA 727
Cdd:COG4717  140 ELAELPERL------------EELEERLEELRE----------------LEEELEELEAELAELQEELEELLEqlslATE 191
                        170       180
                 ....*....|....*....|....
gi 665404360 728 QEISSLQSEIEDLRQRLGESVEIL 751
Cdd:COG4717  192 EELQDLAEELEELQQRLAELEEEL 215
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
556-749 5.19e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 5.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   556 LGKQRKCT-EGEQSDASNS--GDWLALNSELQRSQSQDEELTSLRQRVAELEEELKAAKEGRSltpesrskELETSLEQM 632
Cdd:TIGR02169  636 MGKYRMVTlEGELFEKSGAmtGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELR--------RIENRLDEL 707
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   633 QRAYEDCEdywqtklsEERQLFEKERQIYEDEQHESDKKFTELMEKVREYEEqfskdGRLSPIDERDMLEQQYSELEAEA 712
Cdd:TIGR02169  708 SQELSDAS--------RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ-----EIENVKSELKELEARIEELEEDL 774
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 665404360   713 AQLRSS----SIQMLEEKAQEISSLQSEIEDLRQRLGESVE 749
Cdd:TIGR02169  775 HKLEEAlndlEARLSHSRIPEIQAELSKLEEEVSRIEARLR 815
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
340-572 5.52e-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: 39.75  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 340 VALLAVEVDERHASLEDNSKKQVQQLEQRHASMVREITlRMTNDRDhwtsmtgKLEAQLKSLEQEEIRLRTELELVRTEN 419
Cdd:COG4942    7 LALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELA-ALKKEEK-------ALLKQLAALERRIAALARRIRALEQEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 420 TELESEQQKAHIQITELLEQNIKLNQELAQTSSSIGGTPEHSPLRPRRHSEDKEE--EMLQLM--------EKLAALQME 489
Cdd:COG4942   79 AALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDavRRLQYLkylaparrEQAEELRAD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 490 NAQLRDKTDELTIEIESLNVELIRSKTKAKKQEKQEKQEDQESAATATKRRGDSPSKTHLTEESPRLGKQRKCTEGEQSD 569
Cdd:COG4942  159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238

                 ...
gi 665404360 570 ASN 572
Cdd:COG4942  239 AAE 241
PRK12704 PRK12704
phosphodiesterase; Provisional
591-729 7.63e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 7.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 591 EELTSLRQrvaELEEELKaakegrsltpeSRSKELETSLEQMQRAYEDCEDYWQTkLSEERQLFEKERQIYEDEQHESDK 670
Cdd:PRK12704  64 EEIHKLRN---EFEKELR-----------ERRNELQKLEKRLLQKEENLDRKLEL-LEKREEELEKKEKELEQKQQELEK 128
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360 671 KFTELMEKVREYEEQFSKDGRLSPIDERDM-LEQQYSELEAEAAQLrsssIQMLEEKAQE 729
Cdd:PRK12704 129 KEEELEELIEEQLQELERISGLTAEEAKEIlLEKVEEEARHEAAVL----IKEIEEEAKE 184
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
259-439 7.87e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.04  E-value: 7.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   259 NTRNLLHVLGFDEEEEVNLQQLTKA---LEEELRGIDGDHEQSNMLRALAALQATELGNYRLAYRQQHEENLKLRADNKA 335
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAeeeLAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665404360   336 ANQRVALLAVEVDERHASLEDNSKkQVQQLEQRHASMVREITlRMTNDRDHWT--------------SMTGKLEAQLKSL 401
Cdd:TIGR02168  829 LERRIAATERRLEDLEEQIEELSE-DIESLAAEIEELEELIE-ELESELEALLnerasleealallrSELEELSEELREL 906
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 665404360   402 EQEEIRLRTELELVRTENTELESEQQKAHIQITELLEQ 439
Cdd:TIGR02168  907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
 
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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