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Conserved domains on  [gi|227351255|gb|EEJ41546|]
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hypothetical protein HMPREF0549_0003 [Limosilactobacillus vaginalis DSM 5837 = ATCC 49540]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Surf_Exclu_PgrA super family cl25629
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 218-543 4.32e-18

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


The actual alignment was detected with superfamily member TIGR04320:

Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 87.09  E-value: 4.32e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   218 NYQATDQDKAEKVDPRNMTAAQQTEITKFAAQIVNSFRDSFqstaagaahSYGKVKVSPYATELGNQVIDGAynnsgwnK 297
Cdd:TIGR04320   70 NYKSNAADKNRTVDINNLTDEQQNELSQYAADLINQVRKQL---------GLPPVVVTEGSLDFAQAVAKAY-------K 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   298 SNNATGSPHNENGMVAAANKAGLNTGFvgENLSTGLLLDpaslhrnliQSMSMADVKQSIYAGILAMIYQDVENSAaapl 377
Cdd:TIGR04320  134 KDNSGTGGHDETAINKAAAENGLDNTY--ENLGSISSNN---------ENTTMDDLKRAIYDSILGMLFNDADSNW---- 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   378 yygfgGHTEAFLNDpkgmngisYDDNGNQYMTVTIDKDG--WVHYNFFDDGRASQAVKNKLAQGAITPENASAAQ--INN 453
Cdd:TIGR04320  199 -----GHAQNLLGD--------DKINAGAYLGVSISNDGgvTIHFVNFNDSYIADGNKFDKTPIPNPPNSLAALQakLAT 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   454 AHNDYLQKEGAVTTAQNAATAAQNGVTTAQANVATAQTAVNNATAAQQKAANETLNQ-KAVMANAQAAVNSANENINNLQ 532
Cdd:TIGR04320  266 AQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNLATaQAALANAEARLAKAKEALANLN 345

                          330
                   ....*....|.
gi 227351255   533 AKLAKVQADLN 543
Cdd:TIGR04320  346 ADLAKKQAALD 356
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 482-768 1.66e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.00  E-value: 1.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   482 AQANVATAQTAVNNATAAQQKAANETLNQKAVMANAQAAVNSANENINNLQAKLAKVQAdlnaingsvqdKARQLAQAQT 561
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA-----------EVEQLEERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   562 NLAAAQQKLNASKNVQASR----DAAVNEANAKLNQLQQNVQAKQNDLQQAQSELQNKKNEYSQLNS-----QIRLAKVF 632
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERleeaEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaanlRERLESLE 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   633 GTSLAAVSPQSNYEKAISDAKKAVASAQQKLSDDTQVYKASQAKLQELTATVSQLQTIYEAALSNAKKSDAVQNDAAVKK 712
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227351255   713 AKTALAAAQLKVQVET--GKLTQLKGTLD--------KDQTTLDVA-------NGDLTKAQEKLNSLQNELKR 768
Cdd:TIGR02168  911 SELRRELEELREKLAQleLRLEGLEVRIDnlqerlseEYSLTLEEAealenkiEDDEEEARRRLKRLENKIKE 983
 
Name Accession Description Interval E-value
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 218-543 4.32e-18

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 87.09  E-value: 4.32e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   218 NYQATDQDKAEKVDPRNMTAAQQTEITKFAAQIVNSFRDSFqstaagaahSYGKVKVSPYATELGNQVIDGAynnsgwnK 297
Cdd:TIGR04320   70 NYKSNAADKNRTVDINNLTDEQQNELSQYAADLINQVRKQL---------GLPPVVVTEGSLDFAQAVAKAY-------K 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   298 SNNATGSPHNENGMVAAANKAGLNTGFvgENLSTGLLLDpaslhrnliQSMSMADVKQSIYAGILAMIYQDVENSAaapl 377
Cdd:TIGR04320  134 KDNSGTGGHDETAINKAAAENGLDNTY--ENLGSISSNN---------ENTTMDDLKRAIYDSILGMLFNDADSNW---- 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   378 yygfgGHTEAFLNDpkgmngisYDDNGNQYMTVTIDKDG--WVHYNFFDDGRASQAVKNKLAQGAITPENASAAQ--INN 453
Cdd:TIGR04320  199 -----GHAQNLLGD--------DKINAGAYLGVSISNDGgvTIHFVNFNDSYIADGNKFDKTPIPNPPNSLAALQakLAT 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   454 AHNDYLQKEGAVTTAQNAATAAQNGVTTAQANVATAQTAVNNATAAQQKAANETLNQ-KAVMANAQAAVNSANENINNLQ 532
Cdd:TIGR04320  266 AQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNLATaQAALANAEARLAKAKEALANLN 345

                          330
                   ....*....|.
gi 227351255   533 AKLAKVQADLN 543
Cdd:TIGR04320  346 ADLAKKQAALD 356
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 482-768 1.66e-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: 62.00  E-value: 1.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   482 AQANVATAQTAVNNATAAQQKAANETLNQKAVMANAQAAVNSANENINNLQAKLAKVQAdlnaingsvqdKARQLAQAQT 561
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA-----------EVEQLEERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   562 NLAAAQQKLNASKNVQASR----DAAVNEANAKLNQLQQNVQAKQNDLQQAQSELQNKKNEYSQLNS-----QIRLAKVF 632
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERleeaEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaanlRERLESLE 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   633 GTSLAAVSPQSNYEKAISDAKKAVASAQQKLSDDTQVYKASQAKLQELTATVSQLQTIYEAALSNAKKSDAVQNDAAVKK 712
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227351255   713 AKTALAAAQLKVQVET--GKLTQLKGTLD--------KDQTTLDVA-------NGDLTKAQEKLNSLQNELKR 768
Cdd:TIGR02168  911 SELRRELEELREKLAQleLRLEGLEVRIDnlqerlseEYSLTLEEAealenkiEDDEEEARRRLKRLENKIKE 983
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
480-609 2.61e-09

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 60.06  E-value: 2.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  480 TTAQANVATAQTAVNNATAaQQKAANETLNQKAVMANAQAAVNSANENINNLQAKLAKVQ--ADLNAINGSVQDKAR-QL 556
Cdd:COG1566    79 TDLQAALAQAEAQLAAAEA-QLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQalYKKGAVSQQELDEARaAL 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 227351255  557 AQAQTNLAAAQQKLNASKNvQASRDAAVNEANAKLNQLQQNVQAKQNDLQQAQ 609
Cdd:COG1566   158 DAAQAQLEAAQAQLAQAQA-GLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
PRK11281 PRK11281
mechanosensitive channel MscK;
487-693 5.02e-08

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 57.23  E-value: 5.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  487 ATAQTAVNNATAAQQKAANETLNQKAVMANAQAAVNSANENINNLQAKLAKVQADLNAINGSVQDKARQLAQAQTNLAAa 566
Cdd:PRK11281   27 ARAASNGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEA- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  567 qqklnasknVQASRDAAVNEANAKLN--QLQQNVQAKQNDLQQAQSELqnkkNEY-SQL-NSQIRLAKVfGTSLAAVSPQ 642
Cdd:PRK11281  106 ---------LKDDNDEETRETLSTLSlrQLESRLAQTLDQLQNAQNDL----AEYnSQLvSLQTQPERA-QAALYANSQR 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 227351255  643 S----NYEKAISDAKKAVASAQQKLSDDTQVYKASQAKLQE-LTATVSQLQTIYEA 693
Cdd:PRK11281  172 LqqirNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRkSLEGNTQLQDLLQK 227
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 481-614 1.22e-05

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 48.57  E-value: 1.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   481 TAQANVATAQTAVNNataaQQKAANETLNQKAVMANAQAAVNSANENINNLQAKLAKVQADLN------AING----SVQ 550
Cdd:pfam00529   69 KAQAQVARLQAELDR----LQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLArrrvlaPIGGisreSLV 144

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227351255   551 DKARQLAQAQTNLAAAQQKLN-ASKNVQASRDAAVNEANAKLNQLQQNVQAKQNDLQQAQSELQN 614
Cdd:pfam00529  145 TAGALVAQAQANLLATVAQLDqIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLER 209
PRK11281 PRK11281
mechanosensitive channel MscK;
431-626 4.02e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.52  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  431 AVKNKLAQgaitpenaSAAQINNAHNDyLQKEGAVTTAQNAATAAQNGVTTAQANVATAQTAVNNATAAQQKAANETLNQ 510
Cdd:PRK11281   84 QLKQQLAQ--------APAKLRQAQAE-LEALKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSL 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  511 KAVMANAQAAVNSANENINNLQAKLAKVQADLNAINGSVQDKaRQLAQAQTNLAAAQQKLNASKNV------QASRDaav 584
Cdd:PRK11281  155 QTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVL-LQAEQALLNAQNDLQRKSLEGNTqlqdllQKQRD--- 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 227351255  585 nEANAKLNQLQQNVQAKQ---NDLQQAQSELQNKKNEYSQLNSQI 626
Cdd:PRK11281  231 -YLTARIQRLEHQLQLLQeaiNSKRLTLSEKTVQEAQSQDEAARI 274
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 525-681 7.08e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.70  E-value: 7.08e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255    525 NENINNLQAKLAKVQADLNAINgSVQDKARQLAQAQTNlaAAQQKLNASKNVQASRDAAVNEANAKLNQLQQNVQAKQND 604
Cdd:smart00787  150 DENLEGLKEDYKLLMKELELLN-SIKPKLRDRKDALEE--ELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKK 226

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227351255    605 LQQAQSELQNKKNEYSQLNSQIrlakvfgtslaavspqSNYEKAISDAKKAVASAQQKLSDDTQVYKASQAKLQELT 681
Cdd:smart00787  227 LEELEEELQELESKIEDLTNKK----------------SELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
 
Name Accession Description Interval E-value
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 218-543 4.32e-18

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 87.09  E-value: 4.32e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   218 NYQATDQDKAEKVDPRNMTAAQQTEITKFAAQIVNSFRDSFqstaagaahSYGKVKVSPYATELGNQVIDGAynnsgwnK 297
Cdd:TIGR04320   70 NYKSNAADKNRTVDINNLTDEQQNELSQYAADLINQVRKQL---------GLPPVVVTEGSLDFAQAVAKAY-------K 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   298 SNNATGSPHNENGMVAAANKAGLNTGFvgENLSTGLLLDpaslhrnliQSMSMADVKQSIYAGILAMIYQDVENSAaapl 377
Cdd:TIGR04320  134 KDNSGTGGHDETAINKAAAENGLDNTY--ENLGSISSNN---------ENTTMDDLKRAIYDSILGMLFNDADSNW---- 198

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   378 yygfgGHTEAFLNDpkgmngisYDDNGNQYMTVTIDKDG--WVHYNFFDDGRASQAVKNKLAQGAITPENASAAQ--INN 453
Cdd:TIGR04320  199 -----GHAQNLLGD--------DKINAGAYLGVSISNDGgvTIHFVNFNDSYIADGNKFDKTPIPNPPNSLAALQakLAT 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   454 AHNDYLQKEGAVTTAQNAATAAQNGVTTAQANVATAQTAVNNATAAQQKAANETLNQ-KAVMANAQAAVNSANENINNLQ 532
Cdd:TIGR04320  266 AQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTAQNNLATaQAALANAEARLAKAKEALANLN 345

                          330
                   ....*....|.
gi 227351255   533 AKLAKVQADLN 543
Cdd:TIGR04320  346 ADLAKKQAALD 356
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 482-768 1.66e-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: 62.00  E-value: 1.66e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   482 AQANVATAQTAVNNATAAQQKAANETLNQKAVMANAQAAVNSANENINNLQAKLAKVQAdlnaingsvqdKARQLAQAQT 561
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA-----------EVEQLEERIA 750

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   562 NLAAAQQKLNASKNVQASR----DAAVNEANAKLNQLQQNVQAKQNDLQQAQSELQNKKNEYSQLNS-----QIRLAKVF 632
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERleeaEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEeaanlRERLESLE 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   633 GTSLAAVSPQSNYEKAISDAKKAVASAQQKLSDDTQVYKASQAKLQELTATVSQLQTIYEAALSNAKKSDAVQNDAAVKK 712
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227351255   713 AKTALAAAQLKVQVET--GKLTQLKGTLD--------KDQTTLDVA-------NGDLTKAQEKLNSLQNELKR 768
Cdd:TIGR02168  911 SELRRELEELREKLAQleLRLEGLEVRIDnlqerlseEYSLTLEEAealenkiEDDEEEARRRLKRLENKIKE 983
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
480-609 2.61e-09

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 60.06  E-value: 2.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  480 TTAQANVATAQTAVNNATAaQQKAANETLNQKAVMANAQAAVNSANENINNLQAKLAKVQ--ADLNAINGSVQDKAR-QL 556
Cdd:COG1566    79 TDLQAALAQAEAQLAAAEA-QLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQalYKKGAVSQQELDEARaAL 157

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 227351255  557 AQAQTNLAAAQQKLNASKNvQASRDAAVNEANAKLNQLQQNVQAKQNDLQQAQ 609
Cdd:COG1566   158 DAAQAQLEAAQAQLAQAQA-GLREEEELAAAQAQVAQAEAALAQAELNLARTT 209
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 445-679 1.32e-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: 59.30  E-value: 1.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   445 NASAAQINNAHNDYLQKEGAVTTAQNAATAAQNGVTTAQANVATAQTAVNNATAAQQKAANETLNQKAVMANAQAAVNSA 524
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   525 NENINNLQAKLAKvqADLNAINGSVQDKARQLAQAQTNLAAAQQKLNASKNVQASRDAAVNEANAKLNQLQQNVQAKQND 604
Cdd:TIGR02168  420 QQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227351255   605 LQQAQSELQNKKNeysQLNSQIRLAKVFGTSLAAVSPQSNYEKAISDAkkAVASAQQKLSDDTQVYKASQAKLQE 679
Cdd:TIGR02168  498 QENLEGFSEGVKA---LLKNQSGLSGILGVLSELISVDEGYEAAIEAA--LGGRLQAVVVENLNAAKKAIAFLKQ 567
PRK11281 PRK11281
mechanosensitive channel MscK;
487-693 5.02e-08

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 57.23  E-value: 5.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  487 ATAQTAVNNATAAQQKAANETLNQKAVMANAQAAVNSANENINNLQAKLAKVQADLNAINGSVQDKARQLAQAQTNLAAa 566
Cdd:PRK11281   27 ARAASNGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEA- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  567 qqklnasknVQASRDAAVNEANAKLN--QLQQNVQAKQNDLQQAQSELqnkkNEY-SQL-NSQIRLAKVfGTSLAAVSPQ 642
Cdd:PRK11281  106 ---------LKDDNDEETRETLSTLSlrQLESRLAQTLDQLQNAQNDL----AEYnSQLvSLQTQPERA-QAALYANSQR 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 227351255  643 S----NYEKAISDAKKAVASAQQKLSDDTQVYKASQAKLQE-LTATVSQLQTIYEA 693
Cdd:PRK11281  172 LqqirNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRkSLEGNTQLQDLLQK 227
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 449-703 1.02e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  449 AQINNAHNDYLQKEGAVTTAQNAATAAQNGVTTAQANVATAQTAVNNATAAQQKAANETLNQKAVMANAQAAVNSANENI 528
Cdd:COG1196   267 AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  529 NNLQAKLAKVQADLnaingsvQDKARQLAQAQTNLAAAQQKLNASKNVQASRDAAVNEANAKLNQLQQNVQAKQNDLQQA 608
Cdd:COG1196   347 EEAEEELEEAEAEL-------AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERL 419

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  609 QSELQNKKNEYSQLNSQIrlakvfgtsLAAVSPQSNYEKAISDAKKAVASAQQKLSDDTQVYKASQAKLQELTATVSQLQ 688
Cdd:COG1196   420 EEELEELEEALAELEEEE---------EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490

                         250
                  ....*....|....*
gi 227351255  689 TIYEAALSNAKKSDA 703
Cdd:COG1196   491 ARLLLLLEAEADYEG 505
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 447-770 2.83e-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: 2.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   447 SAAQINNAHNDYLQKEGAVTTAQNAATAAQNGVTTAQANVATAQTAVNNATAAQQKAANETLNQKAVMANAQAAVNSANE 526
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   527 NINNLQAKLAKVQADLnaingsvQDKARQLAQAQTNLAAAQQKLNASKNVQASRDAAVNEANAKLNQLQQNVQAKQNDLQ 606
Cdd:TIGR02168  310 RLANLERQLEELEAQL-------EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   607 QAQSELQNKKNEYSQLNSQIrlakvfgtslaavspqSNYEKAISDAKKAVASAQQKLSDDTQvyKASQAKLQELTATVSQ 686
Cdd:TIGR02168  383 TLRSKVAQLELQIASLNNEI----------------ERLEARLERLEDRRERLQQEIEELLK--KLEEAELKELQAELEE 444

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   687 LQTIYEAAlsnAKKSDAVQNdaavkkaktalaaaqlkvqvetgKLTQLKGTLDKDQTTLDVANGDLTKAQEKLNSLQNEL 766
Cdd:TIGR02168  445 LEEELEEL---QEELERLEE-----------------------ALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498


                   ....
gi 227351255   767 KRAQ 770
Cdd:TIGR02168  499 ENLE 502
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
515-630 8.60e-07

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 51.97  E-value: 8.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  515 ANAQAAVNSANENINNLQAKLAKVQADLNAINGSVQDKArQLAQAQTNLAAAQQKLNASKNVQASR---DAAVNEANAKL 591
Cdd:COG1566    79 TDLQAALAQAEAQLAAAEAQLARLEAELGAEAEIAAAEA-QLAAAQAQLDLAQRELERYQALYKKGavsQQELDEARAAL 157

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 227351255  592 NQLQQNVQAKQNDLQQAQSELQNkKNEYSQLNSQIRLAK 630
Cdd:COG1566   158 DAAQAQLEAAQAQLAQAQAGLRE-EEELAAAQAQVAQAE 195
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 479-688 1.91e-06

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: 51.30  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  479 VTTAQANVATAQTAVNNATAAQQKAANETLNQ-KAVMANAQAAVNSANENINNLQAKLAKVQADLNAINGSVQDKARQLA 557
Cdd:COG4942    14 AAAAQADAAAEAEAELEQLQQEIAELEKELAAlKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  558 QAQTNLAAAQQK--------------------LNASKNVQASRDAA-VNEANAKLNQLQQNVQAKQNDLQQAQSELQNKK 616
Cdd:COG4942    94 ELRAELEAQKEElaellralyrlgrqpplallLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAER 173

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227351255  617 NEYSQLNSQIRLAkvfgtslaavspQSNYEKAISDAKKAVASAQQKLsddtqvyKASQAKLQELTATVSQLQ 688
Cdd:COG4942   174 AELEALLAELEEE------------RAALEALKAERQKLLARLEKEL-------AELAAELAELQQEAEELE 226
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
456-631 2.18e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.56  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  456 NDYLQKEGAVTTAQNAATAAQNGVT-TAQANVATAQTAVNNATAAQQKAANETLNQKAVMANAQAAVNSANENINNLQAK 534
Cdd:COG3206   199 EEFRQKNGLVDLSEEAKLLLQQLSElESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAE 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  535 LAKVQADLNAINGSVQDKARQLAQAQTNLAAAQQK----LNASKNVQASRDAAVNEANAKLNQLQQNVQAKQNDLQQAQS 610
Cdd:COG3206   279 LAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRilasLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLER 358

                         170       180
                  ....*....|....*....|.
gi 227351255  611 ELQNKKNEYSQLNSQIRLAKV 631
Cdd:COG3206   359 EVEVARELYESLLQRLEEARL 379
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 517-701 5.75e-06

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: 49.76  E-value: 5.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  517 AQAAVNSANENINNLQAKLAKVQADLNAINGSVQDKARQLAQAQTNLAAAQQKLNASKNVQASRDAAVNEANAKLNQLQQ 596
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  597 NVQAKQNDLQQAQSELQnKKNEYSQLN-----SQIRLAKVFGTSLAAVSPQSNYE-KAISDAKKAVASAQQKLSDDTQVY 670
Cdd:COG4942    98 ELEAQKEELAELLRALY-RLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQaEELRADLAELAALRAELEAERAEL 176

                         170       180       190
                  ....*....|....*....|....*....|.
gi 227351255  671 KASQAKLQELTATVSQLQTIYEAALSNAKKS 701
Cdd:COG4942   177 EALLAELEEERAALEALKAERQKLLARLEKE 207
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
481-630 6.43e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 6.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  481 TAQANVATAQTAVNNATAAQQKAANE--TLNQKAVMANAQAAVNSANENINNLQAKLAKVQADLNAIngsvQDKARQLAQ 558
Cdd:COG4717    92 ELQEELEELEEELEELEAELEELREEleKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL----RELEEELEE 167

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227351255  559 AQTNLAAAQQKLNASKN-VQASRDAAVNEANAKLNQLQQNVQAKQNDLQQAQSELQNKKNEYSQLNSQIRLAK 630
Cdd:COG4717   168 LEAELAELQEELEELLEqLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 481-614 1.22e-05

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 48.57  E-value: 1.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   481 TAQANVATAQTAVNNataaQQKAANETLNQKAVMANAQAAVNSANENINNLQAKLAKVQADLN------AING----SVQ 550
Cdd:pfam00529   69 KAQAQVARLQAELDR----LQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLArrrvlaPIGGisreSLV 144

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 227351255   551 DKARQLAQAQTNLAAAQQKLN-ASKNVQASRDAAVNEANAKLNQLQQNVQAKQNDLQQAQSELQN 614
Cdd:pfam00529  145 TAGALVAQAQANLLATVAQLDqIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLER 209
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
479-776 1.49e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.36  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  479 VTTAQANVATAQTAVNNATAAQQKAANETLNQKAVMANAQAAVNSANENINNLQAKLAKVQADLNAINGSVQDKARQLAQ 558
Cdd:COG4372    40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  559 AQTNLAAAQQKLNASKNVQASRDAAVNEANAKLNQLQQNVQAKQNDLQQAQSELQNKKNEYS-----QLNSQIRLAKVFG 633
Cdd:COG4372   120 LQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAeqaldELLKEANRNAEKE 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  634 TSLAAVSPQSNYEKAISDAKKAVASAQQKLSDDTQVYKASQAKLQELTATVSQLQTIYEAALSNAKKSDAVQNDAAVKKA 713
Cdd:COG4372   200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227351255  714 KTALAAAQLKVQVETGKLTQLKGTLDKDQTTLDVANGDLTKAQEKLNSLQNELKRAQITLDGL 776
Cdd:COG4372   280 IAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADL 342
PRK11281 PRK11281
mechanosensitive channel MscK;
499-688 1.59e-05

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 49.14  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  499 AQQKAANETLNQKAVMANAQAAVNSANE----NINNLQAKLAKVQADLNAINGSVQDKARQlAQAQTNLAAAQQKLNASK 574
Cdd:PRK11281   56 AEDKLVQQDLEQTLALLDKIDRQKEETEqlkqQLAQAPAKLRQAQAELEALKDDNDEETRE-TLSTLSLRQLESRLAQTL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  575 NVQASRDAAVNEANAKLNQLQQNVQAKQNDLQQAQSELQnkkneysQLNSQIRLAKVFGTSLAAVSPQS-NYEKAISDAK 653
Cdd:PRK11281  135 DQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQ-------QIRNLLKGGKVGGKALRPSQRVLlQAEQALLNAQ 207

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 227351255  654 KAVasAQQKLSDDTQVYKASQAKLQELTATVSQLQ 688
Cdd:PRK11281  208 NDL--QRKSLEGNTQLQDLLQKQRDYLTARIQRLE 240
Tektin pfam03148
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ...
 483-628 4.95e-05

Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.


Pssm-ID: 460827 [Multi-domain]  Cd Length: 383  Bit Score: 46.77  E-value: 4.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   483 QANVATAQTAVNNAtAAQQKAANETLNQKAVMANAQA-AVNSA--------NENINNLQAKLAKVQ-------ADLNAIN 546
Cdd:pfam03148  207 QDNIERAEKERAAS-AQLRELIDSILEQTANDLRAQAdAVNFAlrkrieetEDAKNKLEWQLKKTLqeiaeleKNIEALE 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   547 GSVQDKARQLAQAQTNLAAAQQKlnasKNVQASRDAA----VNEanakLNQLQQNVQAKQNDLQQAQSELQNKKNEYSQL 622
Cdd:pfam03148  286 KAIRDKEAPLKLAQTRLENRTYR----PNVELCRDEAqyglVDE----VKELEETIEALKQKLAEAEASLQALERTRLRL 357


                   ....*.
gi 227351255   623 NSQIRL 628
Cdd:pfam03148  358 EEDIAV 363
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
516-786 1.47e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.78  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  516 NAQAAVNSANENINNLQAKL-AKVQADLNAINGSVQDKARQLAQAQTN-LAAAQQKLNASKNVQASRDAavneanakLNQ 593
Cdd:COG3206   108 DPLGEEASREAAIERLRKNLtVEPVKGSNVIEISYTSPDPELAAAVANaLAEAYLEQNLELRREEARKA--------LEF 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  594 LQQNVQAKQNDLQQAQSELQNKKNEYSQLNSQIRlAKVFGTSLAAVSPQ-SNYEKAISDAKKAVASAQQKLSDDTQ---- 668
Cdd:COG3206   180 LEEQLPELRKELEEAEAALEEFRQKNGLVDLSEE-AKLLLQQLSELESQlAEARAELAEAEARLAALRAQLGSGPDalpe 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  669 -----VYKASQAKLQELTATVSQLQTIY----------EAALSNAKKSDAVQNDAAVKKAKTALAAAQLKVQVETGKLTQ 733
Cdd:COG3206   259 llqspVIQQLRAQLAELEAELAELSARYtpnhpdvialRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQ 338

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 227351255  734 LKG---TLDKDQTTLDVANGDLTKAQEKLNSLQNELKRAQITLDG-------LSHPYIPSTPA 786
Cdd:COG3206   339 LEArlaELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALtvgnvrvIDPAVVPLKPV 401
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 483-767 1.73e-04

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: 45.40  E-value: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   483 QANVATAQTAVNNATAAQQKAANETLNQKAVMANAQAAVNSANENINNLQAKLA-----KVQADLNAINGSVQDKARQLA 557
Cdd:TIGR04523  245 TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISdlnnqKEQDWNKELKSELKNQEKKLE 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   558 QAQTNLAAAQQKLNASKNVQASRDAAVNEANAKLNQLQQNVQAKQNDLQQAQSELQNKKNEYSQLNSQIrlakvfgtsla 637
Cdd:TIGR04523  325 EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQI----------- 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   638 avspqSNYEKAISDAKKAVASAQQKLSDDTQVYKASQAKLQELTATVSQLQtiyeAALSNAKKSDAVQNDAAVKKAKTAL 717
Cdd:TIGR04523  394 -----NDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNN----SEIKDLTNQDSVKELIIKNLDNTRE 464

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 227351255   718 AAAQlKVQVETGKLTQLKGTLDKDQTTLDVANGDLTKAQEKLNSLQNELK 767
Cdd:TIGR04523  465 SLET-QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513
mukB PRK04863
chromosome partition protein MukB;
499-696 1.79e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 45.72  E-value: 1.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  499 AQQKAANETLNQKAVMANAQAAVNSANENINNLQAKLAKVQADLNAINGSVQDKARQLAQAQtnlAAAQQKLNASKNVQA 578
Cdd:PRK04863  408 VQQTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQ---AAHSQFEQAYQLVRK 484

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  579 -----SRDAAVNEANAKLNQL-QQNVQAKQndLQQAQSELQNKKNEYSQLNSQIRLAKVFGTSLAA-VSPQSNYEKAISD 651
Cdd:PRK04863  485 iagevSRSEAWDVARELLRRLrEQRHLAEQ--LQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKnLDDEDELEQLQEE 562

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 227351255  652 AKKAVASAQQKLSDDTQVYKASQAKLQELTATVSQLQTI------YEAALS 696
Cdd:PRK04863  563 LEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARapawlaAQDALA 613
PRK11281 PRK11281
mechanosensitive channel MscK;
431-626 4.02e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.52  E-value: 4.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  431 AVKNKLAQgaitpenaSAAQINNAHNDyLQKEGAVTTAQNAATAAQNGVTTAQANVATAQTAVNNATAAQQKAANETLNQ 510
Cdd:PRK11281   84 QLKQQLAQ--------APAKLRQAQAE-LEALKDDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSL 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  511 KAVMANAQAAVNSANENINNLQAKLAKVQADLNAINGSVQDKaRQLAQAQTNLAAAQQKLNASKNV------QASRDaav 584
Cdd:PRK11281  155 QTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVL-LQAEQALLNAQNDLQRKSLEGNTqlqdllQKQRD--- 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 227351255  585 nEANAKLNQLQQNVQAKQ---NDLQQAQSELQNKKNEYSQLNSQI 626
Cdd:PRK11281  231 -YLTARIQRLEHQLQLLQeaiNSKRLTLSEKTVQEAQSQDEAARI 274
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
483-663 4.54e-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: 4.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  483 QANVATAQTAVNNATAAQQKAANE--TLNQKAVMANAQAAVNSANENINNLQAKLAKVQADLNAI---NGSVQDKARQLA 557
Cdd:COG4913   616 EAELAELEEELAEAEERLEALEAEldALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLdasSDDLAALEEQLE 695

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  558 QAQTNLAAAQQKLnasknvqasrdaavNEANAKLNQLQQNVQAKQNDLQQAQSELQNkKNEYSQLNSQIRLAKVFGTSLA 637
Cdd:COG4913   696 ELEAELEELEEEL--------------DELKGEIGRLEKELEQAEEELDELQDRLEA-AEDLARLELRALLEERFAAALG 760

                         170       180
                  ....*....|....*....|....*....
gi 227351255  638 AVSPQS---NYEKAISDAKKAVASAQQKL 663
Cdd:COG4913   761 DAVERElreNLEERIDALRARLNRAEEEL 789
PRK09039 PRK09039
peptidoglycan -binding protein;
500-629 5.82e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 43.42  E-value: 5.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  500 QQKAANETLNQKAVMANAQAAVNSANEN----INNLQAKLAKVQADLNAINGSVQDKARQLAQAQTNLAAAQQKLNASKN 575
Cdd:PRK09039   51 KDSALDRLNSQIAELADLLSLERQGNQDlqdsVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQ 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 227351255  576 VQASRDAAVNEANAKLNQLQQNVQAKQNDLQQAQSELQNKKNEYSQLNSQIRLA 629
Cdd:PRK09039  131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVA 184
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 525-681 7.08e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.70  E-value: 7.08e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255    525 NENINNLQAKLAKVQADLNAINgSVQDKARQLAQAQTNlaAAQQKLNASKNVQASRDAAVNEANAKLNQLQQNVQAKQND 604
Cdd:smart00787  150 DENLEGLKEDYKLLMKELELLN-SIKPKLRDRKDALEE--ELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKK 226

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 227351255    605 LQQAQSELQNKKNEYSQLNSQIrlakvfgtslaavspqSNYEKAISDAKKAVASAQQKLSDDTQVYKASQAKLQELT 681
Cdd:smart00787  227 LEELEEELQELESKIEDLTNKK----------------SELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLT 287
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 492-615 8.07e-04

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 41.36  E-value: 8.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  492 AVNNATAAQQKAAneTLNQKAVMANAQAAVNSANEninnLQAKLAKVQADLNAINGSVQDKARQLAQAQTNLAAAQqkln 571
Cdd:COG2825    15 ALSAAAAAQLKIG--VVDVQRILQESPEGKAAQKK----LEKEFKKRQAELQKLEKELQALQEKLQKEAATLSEEE---- 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 227351255  572 asknvqasRDAAVNEANAKLNQLQQNVQAKQNDLQQAQSELQNK 615
Cdd:COG2825    85 --------RQKKERELQKKQQELQRKQQEAQQDLQKRQQELLQP 120
PHA03332 PHA03332
membrane glycoprotein; Provisional
 478-664 8.14e-04

membrane glycoprotein; Provisional


Pssm-ID: 223047 [Multi-domain]  Cd Length: 1328  Bit Score: 43.42  E-value: 8.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  478 GVTTAQanVATAQTAVNNATAAQQkAANETLNQKAVMANAQAAVNSANENIN----------------------NLQAKL 535
Cdd:PHA03332  856 GLSAAA--FTMASAALNAATQALA-VATLYVNQLLQATAATAEMASKIGGLNarvdktsdvitklgdtiakisaTLDNNI 932

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  536 AKVQADLNAINGSVQDKARQLAQAQTNLAAAQQKLNASKNvqaSRDAAVNEAnaklNQLQQNVQAKQNDLQQAQSELQNK 615
Cdd:PHA03332  933 RAVNGRVSDLEDQVNLRFLAVATNFNTLATQLKELGTTTN---ERIEEVMAA----ALYYQQLNSLTNQVTQSASKLGYQ 1005

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 227351255  616 KNEYSQLNSQIRLAKVFGTSLAAVSPQSNYEKAISDAKKAVASAQQKLS 664
Cdd:PHA03332 1006 VGMYRTCLKSLLAGTLAGCPTDAPFLRDNPDYTMVKSVYGALYRGQKLF 1054
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
550-761 1.36e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  550 QDKARQLAQAQTNLAAAQQKLNASknvqasrDAAVNEANAKLNQLQQ---------NVQAKQNDLQQAQSELQNKKNEYS 620
Cdd:COG4913   606 FDNRAKLAALEAELAELEEELAEA-------EERLEALEAELDALQErrealqrlaEYSWDEIDVASAEREIAELEAELE 678

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  621 QL-NSQIRLAKVfgtslaavspqsnyEKAISDAKKAVASAQQKLSDDTQVYKASQAKLQELTATVSQLQTIYEAALSNAK 699
Cdd:COG4913   679 RLdASSDDLAAL--------------EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR 744

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 227351255  700 KSDAVQNDAAVKKAKTALAAAQLKvqvetgklTQLKGTLDKDQTTLDVANGDLTKAQEKLNS 761
Cdd:COG4913   745 LELRALLEERFAAALGDAVERELR--------ENLEERIDALRARLNRAEEELERAMRAFNR 798
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 555-689 1.46e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 42.02  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   555 QLAQAQTNLAAAQQKLNASKNVQASRDAAVNEANAKLNQLQQNVQAKQNDLQQAQSELQNKKNEYSQLnsqirlakvfgt 634
Cdd:TIGR04320  248 PIPNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQT------------ 315

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 227351255   635 slaavspqsnyekaisdAKKAVASAQQKLSDDTQVYKASQAKLQELTATVSQLQT 689
Cdd:TIGR04320  316 -----------------AQNNLATAQAALANAEARLAKAKEALANLNADLAKKQA 353
46 PHA02562
endonuclease subunit; Provisional
 516-690 2.21e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.92  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  516 NAQAAVNSANENINNLQAKLAKVQADLNAINGSVQDKARQLAQAQTNL--------------AAAQQKLN------ASKN 575
Cdd:PHA02562  192 HIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELtdellnlvmdiedpSAALNKLNtaaakiKSKI 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  576 VQASRDA--------------AVNEANAKLNQLQQNV---QAKQNDLQQAQSELQNKKNEYSQ-------LNSQIRLAKv 631
Cdd:PHA02562  272 EQFQKVIkmyekggvcptctqQISEGPDRITKIKDKLkelQHSLEKLDTAIDELEEIMDEFNEqskklleLKNKISTNK- 350

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  632 fgTSLaavspqSNYEKAISDAKKAVasaqQKLSDDTQVYKASQAKLQ-ELTATVSQLQTI 690
Cdd:PHA02562  351 --QSL------ITLVDKAKKVKAAI----EELQAEFVDNAEELAKLQdELDKIVKTKSEL 398
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
482-626 2.69e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  482 AQANVATAQTAVNNATAAQQKAANETLNQKAVMANAQAAVNSANENINNLQAKLAKV--------QADLNAINGSVQDKA 553
Cdd:COG4913   279 AALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrleqlEREIERLERELEERE 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  554 RQLAQAQTNLAAAQQKLNAS----KNVQASRDAAVNEANAKLNQLQQNV---QAKQNDLQQAQSELQNKKNEYSQLNSQI 626
Cdd:COG4913   359 RRRARLEALLAALGLPLPASaeefAALRAEAAALLEALEEELEALEEALaeaEAALRDLRRELRELEAEIASLERRKSNI 438
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 532-611 2.92e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 41.86  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  532 QAKLAKVQADLNAINGSVQDKARQLAQAQTNLAAAQQKLNASKNVQASRDAAVNEANAKLNQLQQNVQAKQNDLQQAQSE 611
Cdd:PRK11448  141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKE 220
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
444-659 3.81e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 3.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  444 ENASAAQINNAHNDYLQKEGAVTTAQNAATAAQNGVTTAQANVATAQTAVNNATAAQQKAANETLN-QKAVMANAQAAVN 522
Cdd:COG4913   262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDElEAQIRGNGGDRLE 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  523 SANENINNLQAKLAKVQadlnaingsvqdkaRQLAQAQTNLAAAQQKLNAS----KNVQASRDAAVNEANAKLNQLQQNV 598
Cdd:COG4913   342 QLEREIERLERELEERE--------------RRRARLEALLAALGLPLPASaeefAALRAEAAALLEALEEELEALEEAL 407

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 227351255  599 QAKQNDLQQAQSELQNKKNEYSQLNSQirlakvfgtslaavspQSNYEKAISDAKKAVASA 659
Cdd:COG4913   408 AEAEAALRDLRRELRELEAEIASLERR----------------KSNIPARLLALRDALAEA 452
PRK10476 PRK10476
multidrug transporter subunit MdtN;
479-614 4.41e-03

multidrug transporter subunit MdtN;


Pssm-ID: 182488 [Multi-domain]  Cd Length: 346  Bit Score: 40.40  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  479 VTTAQANVATAQTAVNNAT---AAQQKAANETlnqKAVMANAQAAVNSANENINNLQAKLAKvqadlnainGSVqdKARQ 555
Cdd:PRK10476   88 VAQAQADLALADAQIMTTQrsvDAERSNAASA---NEQVERARANAKLATRTLERLEPLLAK---------GYV--SAQQ 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 227351255  556 LAQAQTNLAAAQQKLNASKNVQASRDAAVNEANAKLNQlqqnVQAKQNDLQQAQSELQN 614
Cdd:PRK10476  154 VDQARTAQRDAEVSLNQALLQAQAAAAAVGGVDALVAQ----RAAREAALAIAELHLED 208
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
589-770 4.87e-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: 4.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  589 AKLNQLQQNVQAKQNDLQQAQSELQNKKNEYSQLNSQIRLakvfgtsLAAVSPQSNYEKAISDAKKAVASAQQKLSDdtq 668
Cdd:COG4913   610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREA-------LQRLAEYSWDEIDVASAEREIAELEAELER--- 679

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  669 vYKASQAKLQELTATVSQLQTIYEAAlsnAKKSDAVQ-------------NDAAVKKAKTALAAAQLKVQVETGKLTQLK 735
Cdd:COG4913   680 -LDASSDDLAALEEQLEELEAELEEL---EEELDELKgeigrlekeleqaEEELDELQDRLEAAEDLARLELRALLEERF 755

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 227351255  736 GTLDKDQTTLDVA---NGDLTKAQEKLNSLQNELKRAQ 770
Cdd:COG4913   756 AAALGDAVERELRenlEERIDALRARLNRAEEELERAM 793
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 521-706 6.09e-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: 40.39  E-value: 6.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   521 VNSANENINNLQAKLAKVQADLNAINGSVQDKARQLAQAQTNLAAAQQKLNASKNvqasrdaAVNEANAKLNQLqqNVQA 600
Cdd:TIGR04523  234 IEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK-------QLNQLKSEISDL--NNQK 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255   601 KQNDLQQAQSELQNKKNEYSQLNSQIrlakvfgtslaavspqSNYEKAISDAKKAVASAQQKLSDDTQvykASQAKLQEL 680
Cdd:TIGR04523  305 EQDWNKELKSELKNQEKKLEEIQNQI----------------SQNNKIISQLNEQISQLKKELTNSES---ENSEKQREL 365

                          170       180
                   ....*....|....*....|....*.
gi 227351255   681 TATVSQLQTIYEaalSNAKKSDAVQN 706
Cdd:TIGR04523  366 EEKQNEIEKLKK---ENQSYKQEIKN 388
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 586-701 6.31e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.58  E-value: 6.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  586 EANAKLNQLQQNVQAKQNDLQQAQSELQNKKNE----YSQLNSQI-RLAKVFGTSLAAVspQSNYEKAISDAKKAVASAQ 660
Cdd:PRK00409  513 EDKEKLNELIASLEELERELEQKAEEAEALLKEaeklKEELEEKKeKLQEEEDKLLEEA--EKEAQQAIKEAKKEADEII 590

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 227351255  661 QKLSDDTQVYKASQaKLQELTATVSQLQTIYEAALSNAKKS 701
Cdd:PRK00409  591 KELRQLQKGGYASV-KAHELIEARKRLNKANEKKEKKKKKQ 630
PRK06975 PRK06975
bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed
 499-595 6.37e-03

bifunctional uroporphyrinogen-III synthetase/uroporphyrin-III C-methyltransferase; Reviewed


Pssm-ID: 235899 [Multi-domain]  Cd Length: 656  Bit Score: 40.47  E-value: 6.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  499 AQQKAANETLNQKAVM--ANAQAAVNSANENINNLQAKLAKVQADLNAINGSVQDKAR-----QLAQAQTNLAAAQQKLN 571
Cdd:PRK06975  356 VQRQQANDAQTAELRVktEQAQASVHQLDSQFAQLDGKLADAQSAQQALEQQYQDLSRnrddwMIAEVEQMLSSASQQLQ 435

                          90       100
                  ....*....|....*....|....
gi 227351255  572 ASKNVQASRdAAVNEANAKLNQLQ 595
Cdd:PRK06975  436 LTGNVQLAL-IALQNADARLATSD 458
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
482-768 8.08e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 8.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  482 AQANVATAQTAVNNATAAQQKAANETLNQKAVMANAQAAVNSANENINNLQAKLAKVQADLNAINGSVQDKARQLAQAQT 561
Cdd:COG4372    78 LEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  562 NLAAAQQKLNASKNV-----QASRDAAVNEANAKLNQLQQNVQAKQNDLQQAQSELQNKKNEYSQLNSQIRLAKVFGTSL 636
Cdd:COG4372   158 QLESLQEELAALEQElqalsEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSA 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  637 AAVSPQSNYEKAISDAKKAVASAQQKLSDDTQVYKASQAKLQELTATVSQLQTIYEAALSNAKKSDAVQNDAAVKKAKTA 716
Cdd:COG4372   238 LLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDAL 317

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 227351255  717 LAAAQLKVQVETGKLTQLKGTLDKDQTTLDVANGDLTKAQEKLNSLQNELKR 768
Cdd:COG4372   318 LAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
PRK05035 PRK05035
electron transport complex protein RnfC; Provisional
 483-706 8.12e-03

electron transport complex protein RnfC; Provisional


Pssm-ID: 235334 [Multi-domain]  Cd Length: 695  Bit Score: 39.93  E-value: 8.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  483 QANVATAQTAVNNATAAQQKAANETLNQKAVMANAQAAVNSANENINNLQA------KLAKVQAdlnAIngsvqdkarql 556
Cdd:PRK05035  489 AAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAaaaadpKKAAVAA---AI----------- 554

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  557 AQAQTNLAAAQQKLNASKNVQASRDAAVNEANAKLNQLQQNVQAKQNDLQQAQSELQNKKNEYSQLNSQIRLAKVFGTSL 636
Cdd:PRK05035  555 ARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQAN 634

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  637 AAVSPQSNYEKAIsdAKKAVASAQQKLsddtqvyKASQAKLQELTATVSQLQTIYEAALSNAKKSDAVQN 706
Cdd:PRK05035  635 AEPEEPVDPRKAA--VAAAIARAKARK-------AAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
582-777 8.38e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 8.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  582 AAVNEANAKLNQLQQNV---QAKQNDLQQAQSELQNKKNEYSQLNSQIRLAKvfgtslaavspqsnYEKAISDAKKAVAS 658
Cdd:COG4717    71 KELKELEEELKEAEEKEeeyAELQEELEELEEELEELEAELEELREELEKLE--------------KLLQLLPLYQELEA 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  659 AQQKLSDDTQVYKASQAKLQELTATVSQLQTIyEAALSNAKKSDAVQNDAAVKKAKTALAAAQLKVQVETGKLTQLKGTL 738
Cdd:COG4717   137 LEAELAELPERLEELEERLEELRELEEELEEL-EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 227351255  739 DKDQTTLDVANGDLTKAQEKLNSLQ--NELKRAQITLDGLS 777
Cdd:COG4717   216 EEAQEELEELEEELEQLENELEAAAleERLKEARLLLLIAA 256
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
507-630 8.52e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 8.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  507 TLNQKAVMANAQAAVNSANENINNLqakLAKVQADLNAINGSVQDKARQLAQAQTNLAAAQQKLNASKNVQASRDAAVNE 586
Cdd:COG4717   351 ELLREAEELEEELQLEELEQEIAAL---LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE 427

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 227351255  587 AN--AKLNQLQQNVQAKQNDLQQAQSELQNKKNEYSQLNSQIRLAK 630
Cdd:COG4717   428 EEleEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
PRK12704 PRK12704
phosphodiesterase; Provisional
 499-624 8.59e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 8.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  499 AQQKAANETLNQKAVMANAQAAVNSANENINnLQAK------LAKVQADLNAINGSVQDKARQLAQAQTNLAAAQQKLNa 572
Cdd:PRK12704   29 AEAKIKEAEEEAKRILEEAKKEAEAIKKEAL-LEAKeeihklRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLE- 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 227351255  573 sknvqaSRDAAVNEANAKLNQLQQNVQAKQNDLQQAQSELQNKKNEYSQLNS 624
Cdd:PRK12704  107 ------KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTA 152
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
508-768 9.20e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 9.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  508 LNQKAVMANAQAAVNSAnENINNLQAKLAKVQADLNAInGSVQDKARQLAQAQTNLAAAQQKLNASKNVQASRdaAVNEA 587
Cdd:COG4913   218 LEEPDTFEAADALVEHF-DDLERAHEALEDAREQIELL-EPIRELAERYAAARERLAELEYLRAALRLWFAQR--RLELL 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  588 NAKLNQLQQNVQAKQNDLQQAQSELQNKKNEYSQLNSQIRlakvfgtslaavspQSNYEKaISDAKKAVASAQQKLSDDT 667
Cdd:COG4913   294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIR--------------GNGGDR-LEQLEREIERLERELEERE 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 227351255  668 QVYKASQAKLQELTATVSQLQTIYEAALSNAKKSDAvqndaavkkaktalaaaqlkvqvetgKLTQLKGTLDKDQTTLDV 747
Cdd:COG4913   359 RRRARLEALLAALGLPLPASAEEFAALRAEAAALLE--------------------------ALEEELEALEEALAEAEA 412

                         250       260
                  ....*....|....*....|.
gi 227351255  748 AngdLTKAQEKLNSLQNELKR 768
Cdd:COG4913   413 A---LRDLRRELRELEAEIAS 430
 
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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