NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|737779514|ref|WP_035747364|]
View 

plasmid recombination protein [Haematobacter missouriensis]

Protein Classification

plasmid recombination protein( domain architecture ID 15322803)

plasmid recombination protein belongs to the plasmid mobilization pre family

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MobM_relaxase cd17242
relaxase domain of MobM and similar proteins; With some plasmids, recombination can occur in a ...
 20-196 9.25e-19

relaxase domain of MobM and similar proteins; With some plasmids, recombination can occur in a site-specific manner that is independent of RecA. In such cases, the recombination event requires another protein called Pre (plasmid recombination enzyme), also known as Mob (conjugative mobilization). The best characterized member of this family is encoded by the streptococcal plasmid pMV158 that recognizes the plasmid origin of transfer. MobM converts supercoiled plasmid DNA into relaxed DNA by cleaving a phosphodiester bond of a specific dinucleotide and remains bound to the 5'-end of the nick site.


:

Pssm-ID: 410988  Cd Length: 196  Bit Score: 83.47  E-value: 9.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  20 RIKGRNATAAGGQRAHDMR-MGPQPAYVDQSRSHLNRVLMEPKTGAQLRAIsEKRRALRDTARGMKSNASVAIVGIITFG 98
Cdd:cd17242    3 RVEKLKSGALGGALRHNEReRETENPNIDPSRTHLNYELVGPGKKDYAEAI-KERLEELGKKKKIRKDAVLAVEFILTAS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  99 HEAqiiFEKLTPEQQDAAYWETAEAIATRL-NSPLTGLVAHADESAPHAHF---------QLPAYDLTGhpisetaKRGV 168
Cdd:cd17242   82 PEF---FEGLDPEEIEEFFKDALEFLKERFgEENIVSAVVHLDETTPHLHAvvvpitedgRLSAKELFG-------GRKK 151

                        170       180
                 ....*....|....*....|....*...
gi 737779514 169 LREIQTLTGEIMGRHApGIERGNSKASR 196
Cdd:cd17242  152 LRELQDDYAEAVAKKG-GLERGIKGSKA 178
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 187-374 9.23e-10

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: 60.46  E-value: 9.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514   187 IERGNSKASRLQAGASPADVVNRQVNQLHAELPAEIAAKEAERDAVQADLEKHQRHL---TKAKADLEKAIAQTGEESA- 262
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalREALDELRAELTLLNEEAAn 821

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514   263 ---KVETISKRAATYEKRVKTAQAELERLTLEQAAQQAALDKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTS 339
Cdd:TIGR02168  822 lreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 737779514   340 ELDGLNNAVAQKKTNIESLLTRKAALEASLQSLRA 374
Cdd:TIGR02168  902 ELRELESKRSELRRELEELREKLAQLELRLEGLEV 936
 
Name Accession Description Interval E-value
MobM_relaxase cd17242
relaxase domain of MobM and similar proteins; With some plasmids, recombination can occur in a ...
 20-196 9.25e-19

relaxase domain of MobM and similar proteins; With some plasmids, recombination can occur in a site-specific manner that is independent of RecA. In such cases, the recombination event requires another protein called Pre (plasmid recombination enzyme), also known as Mob (conjugative mobilization). The best characterized member of this family is encoded by the streptococcal plasmid pMV158 that recognizes the plasmid origin of transfer. MobM converts supercoiled plasmid DNA into relaxed DNA by cleaving a phosphodiester bond of a specific dinucleotide and remains bound to the 5'-end of the nick site.


Pssm-ID: 410988  Cd Length: 196  Bit Score: 83.47  E-value: 9.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  20 RIKGRNATAAGGQRAHDMR-MGPQPAYVDQSRSHLNRVLMEPKTGAQLRAIsEKRRALRDTARGMKSNASVAIVGIITFG 98
Cdd:cd17242    3 RVEKLKSGALGGALRHNEReRETENPNIDPSRTHLNYELVGPGKKDYAEAI-KERLEELGKKKKIRKDAVLAVEFILTAS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  99 HEAqiiFEKLTPEQQDAAYWETAEAIATRL-NSPLTGLVAHADESAPHAHF---------QLPAYDLTGhpisetaKRGV 168
Cdd:cd17242   82 PEF---FEGLDPEEIEEFFKDALEFLKERFgEENIVSAVVHLDETTPHLHAvvvpitedgRLSAKELFG-------GRKK 151

                        170       180
                 ....*....|....*....|....*...
gi 737779514 169 LREIQTLTGEIMGRHApGIERGNSKASR 196
Cdd:cd17242  152 LRELQDDYAEAVAKKG-GLERGIKGSKA 178
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 187-374 9.23e-10

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: 60.46  E-value: 9.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514   187 IERGNSKASRLQAGASPADVVNRQVNQLHAELPAEIAAKEAERDAVQADLEKHQRHL---TKAKADLEKAIAQTGEESA- 262
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalREALDELRAELTLLNEEAAn 821

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514   263 ---KVETISKRAATYEKRVKTAQAELERLTLEQAAQQAALDKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTS 339
Cdd:TIGR02168  822 lreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 737779514   340 ELDGLNNAVAQKKTNIESLLTRKAALEASLQSLRA 374
Cdd:TIGR02168  902 ELRELESKRSELRRELEELREKLAQLELRLEGLEV 936
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 220-374 1.56e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 220 AEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELERLTLEQAAQQAAL 299
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 737779514 300 DKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDGLNNAVAQKKTNIESLLTRKAALEASLQSLRA 374
Cdd:COG1196  340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
Mob_Pre pfam01076
Plasmid recombination enzyme; With some plasmids, recombination can occur in a site specific ...
 46-196 1.18e-07

Plasmid recombination enzyme; With some plasmids, recombination can occur in a site specific manner that is independent of RecA. In such cases, the recombination event requires another protein called Pre. Pre is a plasmid recombination enzyme. This protein is also known as Mob (conjugative mobilization). This family is also known as Mob-V. One of the family members, MobM, is encoded by a promiscuous plasmid actively involved in the spread of antibiotic resistance. Homologs of MobM are found in many plasmids and other mobile genetic elements of pathogenic bacteria, including S. aureus. MobM is a metal-dependent nuclease that uses histidine nitrogen for the nucleophilic attack on the scissile phosphate. Furthermore, in contrast to other DNA-processing enzymes, MobM is a histidine relaxase, a DNA-breaking and -joining enzyme, that operates through a phosphorus-nitrogen protein-DNA adduct for cell-to-cell DNA transfer. Mutational analysis indicate that the H(N/D)(Q/E)R N-terminal motif of MobM plays a crucial role in the cleavage and generation of stable DNA-protein adducts.


Pssm-ID: 395854  Cd Length: 195  Bit Score: 51.55  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514   46 VDQSRSHLNRVLMEPKTGAQLRAISEKRRALRDTARGMKSNASVAIVGIITFGHEaqiIFEKLTPEQQDAAYWETAEAIA 125
Cdd:pfam01076  35 IDPERSGLNYDLVNDKQIRYDEDIKDYIKENQKSKRKIRKDAVLENEILITSDPD---FFEQLTYEEAKEFFETAFQFFE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  126 TRL-NSPLTGLVAHADESAPHAHFQ---------LPAYDLTGhpisetaKRGVLREIQTLTGEIMGRHAPGIERGNSKAS 195
Cdd:pfam01076 112 ERYgKENVLYAVVHLDEATPHMHMGvvpgtedgrLSAKAIFG-------NRKELIALQDRFPEYMGLKGFDLERGEPGSE 184


                  .
gi 737779514  196 R 196
Cdd:pfam01076 185 R 185
MobV NF041497
MobV family relaxase;
1-192 1.47e-07

MobV family relaxase;


Pssm-ID: 469385  Cd Length: 187  Bit Score: 51.03  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514   1 MSGEVMRPEKggnpraaqtrIKGRNATAAGgqrAHDMRMGPQ--PAYVDQSRSHLNRVLMEPKTGAQ--LRAISEKRRAL 76
Cdd:NF041497   1 MSYAVLRVEK----------LKGGNLAGSQ---EHNERETENrtNPNADPSRTHLNFELVNGPDGPIdyLEAIKERIAEN 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  77 RDTARGMKSNASVAIVGIITFGHEAqiiFEKLTPEQQDAAYWETA----------EAIAtrlnspltGLVAHADESAPHA 146
Cdd:NF041497  68 AGIKRKIRKDAVRAVEFILTGSPEF---FKELADPGELKEWFEDNydfladrygeENIV--------SAVVHLDETTPHI 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 737779514 147 HFQLPaydltghPISETAK--------RGVLREIQTLTGEIMGRHapGIERGNS 192
Cdd:NF041497 137 HATVV-------PITEDGRlsakdvfgRKKLSQLQDDYAEAMKKY--GLERGIS 181
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
216-373 1.17e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.34  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 216 AELPAEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELE--RLTLEQA 293
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecRVAAQAH 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 294 AQQA-----ALDKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDGLNNAVAQKKTNIESLLTRKAALEAS 368
Cdd:PRK02224 341 NEEAeslreDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREE 420


                 ....*
gi 737779514 369 LQSLR 373
Cdd:PRK02224 421 RDELR 425
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 217-353 6.15e-05

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 44.99  E-value: 6.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  217 ELPAEIAAKEAER-----DAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELERLTLE 291
Cdd:pfam05262 205 ERESQEDAKRAQQlkeelDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIE 284

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 737779514  292 QAAQQA--ALDKINRGKEKAQDELSQ-IKGQQVEARADLAEVETRRAETTSELDGLNNAVAQKKT 353
Cdd:pfam05262 285 KAQIEIkkNDEEALKAKDHKAFDLKQeSKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPT 349
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 230-373 8.92e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 37.73  E-value: 8.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 230 DAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKR---------AATYEKRVKTAQAELERLTLEQAAQ-QAAL 299
Cdd:cd22656  124 DDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKAlkdlltdegGAIARKEIKDLQKELEKLNEEYAAKlKAKI 203

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737779514 300 DKINRGKEKAQDELSQIKgqqvEARADLAEVETrraettsELDGLNNAVAQKKTNIESLLTRKAALEASLQSLR 373
Cdd:cd22656  204 DELKALIADDEAKLAAAL----RLIADLTAADT-------DLDNLLALIGPAIPALEKLQGAWQAIATDLDSLK 266
 
Name Accession Description Interval E-value
MobM_relaxase cd17242
relaxase domain of MobM and similar proteins; With some plasmids, recombination can occur in a ...
 20-196 9.25e-19

relaxase domain of MobM and similar proteins; With some plasmids, recombination can occur in a site-specific manner that is independent of RecA. In such cases, the recombination event requires another protein called Pre (plasmid recombination enzyme), also known as Mob (conjugative mobilization). The best characterized member of this family is encoded by the streptococcal plasmid pMV158 that recognizes the plasmid origin of transfer. MobM converts supercoiled plasmid DNA into relaxed DNA by cleaving a phosphodiester bond of a specific dinucleotide and remains bound to the 5'-end of the nick site.


Pssm-ID: 410988  Cd Length: 196  Bit Score: 83.47  E-value: 9.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  20 RIKGRNATAAGGQRAHDMR-MGPQPAYVDQSRSHLNRVLMEPKTGAQLRAIsEKRRALRDTARGMKSNASVAIVGIITFG 98
Cdd:cd17242    3 RVEKLKSGALGGALRHNEReRETENPNIDPSRTHLNYELVGPGKKDYAEAI-KERLEELGKKKKIRKDAVLAVEFILTAS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  99 HEAqiiFEKLTPEQQDAAYWETAEAIATRL-NSPLTGLVAHADESAPHAHF---------QLPAYDLTGhpisetaKRGV 168
Cdd:cd17242   82 PEF---FEGLDPEEIEEFFKDALEFLKERFgEENIVSAVVHLDETTPHLHAvvvpitedgRLSAKELFG-------GRKK 151

                        170       180
                 ....*....|....*....|....*...
gi 737779514 169 LREIQTLTGEIMGRHApGIERGNSKASR 196
Cdd:cd17242  152 LRELQDDYAEAVAKKG-GLERGIKGSKA 178
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 187-374 9.23e-10

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: 60.46  E-value: 9.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514   187 IERGNSKASRLQAGASPADVVNRQVNQLHAELPAEIAAKEAERDAVQADLEKHQRHL---TKAKADLEKAIAQTGEESA- 262
Cdd:TIGR02168  742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELkalREALDELRAELTLLNEEAAn 821

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514   263 ---KVETISKRAATYEKRVKTAQAELERLTLEQAAQQAALDKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTS 339
Cdd:TIGR02168  822 lreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 737779514   340 ELDGLNNAVAQKKTNIESLLTRKAALEASLQSLRA 374
Cdd:TIGR02168  902 ELRELESKRSELRRELEELREKLAQLELRLEGLEV 936
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 220-374 1.56e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 220 AEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELERLTLEQAAQQAAL 299
Cdd:COG1196  260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 737779514 300 DKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDGLNNAVAQKKTNIESLLTRKAALEASLQSLRA 374
Cdd:COG1196  340 EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 209-369 1.93e-09

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: 57.24  E-value: 1.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 209 RQVNQLHAELPAEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAiaqtgeeSAKVETISKRAATYEKRVKTAQA--ELE 286
Cdd:COG1579   20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL-------ELEIEEVEARIKKYEEQLGNVRNnkEYE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 287 RLTLEQAAQQAALDKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDglnNAVAQKKTNIESLLTRKAALE 366
Cdd:COG1579   93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD---EELAELEAELEELEAEREELA 169


                 ...
gi 737779514 367 ASL 369
Cdd:COG1579  170 AKI 172
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 209-374 2.60e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.79  E-value: 2.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 209 RQVNQLHAELPAEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELERL 288
Cdd:COG1196  235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 289 TLEQAAQQAALDKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDGLNNAVAQKKTNIESLLTRKAALEAS 368
Cdd:COG1196  315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394


                 ....*.
gi 737779514 369 LQSLRA 374
Cdd:COG1196  395 AAELAA 400
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
193-374 6.31e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 57.62  E-value: 6.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  193 KASRLQAGASPADVVNRQvnQLHAELPAEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQTGEESakvetiSKRAA 272
Cdd:COG4913   270 RLAELEYLRAALRLWFAQ--RRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNG------GDRLE 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  273 TYEKRVKTAQAELERLTLEQAAQQAALDKINRGKEKAQDEL----SQIKGQQVEARADLAEVETRRAETTSELDGLNNAV 348
Cdd:COG4913   342 QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFaalrAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421

                         170       180
                  ....*....|....*....|....*.
gi 737779514  349 AQKKTNIESLLTRKAALEASLQSLRA 374
Cdd:COG4913   422 RELEAEIASLERRKSNIPARLLALRD 447
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 209-374 1.33e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 209 RQVNQLHAELPAEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELERL 288
Cdd:COG1196  263 AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 289 TLEQAAQQAALDKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDGLNNAVAQKKTNIESLLTRKAALEAS 368
Cdd:COG1196  343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422


                 ....*.
gi 737779514 369 LQSLRA 374
Cdd:COG1196  423 LEELEE 428
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 191-374 1.89e-08

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: 1.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 191 NSKASRLQAGASPADVVNRQVNQLHAELPAEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKR 270
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 271 AATYEKRVKTAQAELERLTLEQAAQQAALDKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDGLNNAVAQ 350
Cdd:COG1196  374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453

                        170       180
                 ....*....|....*....|....
gi 737779514 351 KKTNIESLLTRKAALEASLQSLRA 374
Cdd:COG1196  454 LEEEEEALLELLAELLEEAALLEA 477
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 163-374 3.49e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 3.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 163 TAKRGVLREIQTLTGEIMGRHAPGIERGNSKASRLQAGASPADVVNRQVNQLHAELP---AEIAAKEAERDAVQADLEKH 239
Cdd:COG1196  284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEeleEELEEAEEELEEAEAELAEA 363

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 240 QRHLTKAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELERLTLEQAAQQAALDKINRGKEKAQDELSQIKGQ 319
Cdd:COG1196  364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 737779514 320 QVEARADLAEVETRRAETTSELDGLNNAVAQKKTNIESLLTRKAALEASLQSLRA 374
Cdd:COG1196  444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 207-374 7.57e-08

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: 7.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 207 VNRQVNQLHAElpaeiaAKEAER-DAVQADLEKHQRHLTKAKadLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAEL 285
Cdd:COG1196  198 LERQLEPLERQ------AEKAERyRELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAEL 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 286 ERLTLEQAAQQAALDKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDGLNNAVAQKKTNIESLLTRKAAL 365
Cdd:COG1196  270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349


                 ....*....
gi 737779514 366 EASLQSLRA 374
Cdd:COG1196  350 EEELEEAEA 358
Mob_Pre pfam01076
Plasmid recombination enzyme; With some plasmids, recombination can occur in a site specific ...
 46-196 1.18e-07

Plasmid recombination enzyme; With some plasmids, recombination can occur in a site specific manner that is independent of RecA. In such cases, the recombination event requires another protein called Pre. Pre is a plasmid recombination enzyme. This protein is also known as Mob (conjugative mobilization). This family is also known as Mob-V. One of the family members, MobM, is encoded by a promiscuous plasmid actively involved in the spread of antibiotic resistance. Homologs of MobM are found in many plasmids and other mobile genetic elements of pathogenic bacteria, including S. aureus. MobM is a metal-dependent nuclease that uses histidine nitrogen for the nucleophilic attack on the scissile phosphate. Furthermore, in contrast to other DNA-processing enzymes, MobM is a histidine relaxase, a DNA-breaking and -joining enzyme, that operates through a phosphorus-nitrogen protein-DNA adduct for cell-to-cell DNA transfer. Mutational analysis indicate that the H(N/D)(Q/E)R N-terminal motif of MobM plays a crucial role in the cleavage and generation of stable DNA-protein adducts.


Pssm-ID: 395854  Cd Length: 195  Bit Score: 51.55  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514   46 VDQSRSHLNRVLMEPKTGAQLRAISEKRRALRDTARGMKSNASVAIVGIITFGHEaqiIFEKLTPEQQDAAYWETAEAIA 125
Cdd:pfam01076  35 IDPERSGLNYDLVNDKQIRYDEDIKDYIKENQKSKRKIRKDAVLENEILITSDPD---FFEQLTYEEAKEFFETAFQFFE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  126 TRL-NSPLTGLVAHADESAPHAHFQ---------LPAYDLTGhpisetaKRGVLREIQTLTGEIMGRHAPGIERGNSKAS 195
Cdd:pfam01076 112 ERYgKENVLYAVVHLDEATPHMHMGvvpgtedgrLSAKAIFG-------NRKELIALQDRFPEYMGLKGFDLERGEPGSE 184


                  .
gi 737779514  196 R 196
Cdd:pfam01076 185 R 185
MobV NF041497
MobV family relaxase;
1-192 1.47e-07

MobV family relaxase;


Pssm-ID: 469385  Cd Length: 187  Bit Score: 51.03  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514   1 MSGEVMRPEKggnpraaqtrIKGRNATAAGgqrAHDMRMGPQ--PAYVDQSRSHLNRVLMEPKTGAQ--LRAISEKRRAL 76
Cdd:NF041497   1 MSYAVLRVEK----------LKGGNLAGSQ---EHNERETENrtNPNADPSRTHLNFELVNGPDGPIdyLEAIKERIAEN 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  77 RDTARGMKSNASVAIVGIITFGHEAqiiFEKLTPEQQDAAYWETA----------EAIAtrlnspltGLVAHADESAPHA 146
Cdd:NF041497  68 AGIKRKIRKDAVRAVEFILTGSPEF---FKELADPGELKEWFEDNydfladrygeENIV--------SAVVHLDETTPHI 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 737779514 147 HFQLPaydltghPISETAK--------RGVLREIQTLTGEIMGRHapGIERGNS 192
Cdd:NF041497 137 HATVV-------PITEDGRlsakdvfgRKKLSQLQDDYAEAMKKY--GLERGIS 181
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 216-372 2.77e-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: 52.75  E-value: 2.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514   216 AELPAEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELERLTLEQAAQ 295
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514   296 QAALdkinrgkEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDGLNNAV-------AQKKTNIESLLTRKAALEAS 368
Cdd:TIGR02168  767 EERL-------EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllneeaANLRERLESLERRIAATERR 839


                   ....
gi 737779514   369 LQSL 372
Cdd:TIGR02168  840 LEDL 843
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 217-372 3.57e-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: 52.37  E-value: 3.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514   217 ELPAEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKR-------AATYEKRVKTAQAELERLT 289
Cdd:TIGR02168  236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyalaneISRLEQQKQILRERLANLE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514   290 LEQAAQQAALDKINRGKEKAQDELSQIK--------------GQQVEARADLAEVETRRAETTSELDGLNNAVAQKKTNI 355
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELAELEekleelkeelesleAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395

                          170
                   ....*....|....*..
gi 737779514   356 ESLLTRKAALEASLQSL 372
Cdd:TIGR02168  396 ASLNNEIERLEARLERL 412
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
222-367 6.05e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.45  E-value: 6.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  222 IAAKEAERDAVQADLEKHQRHLTKAKADLEkAIAQTGEESAKVETISKRaatyEKRVKTAQAELERLtleqaaqQAALDK 301
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELD-ALQERREALQRLAEYSWD----EIDVASAEREIAEL-------EAELER 679

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 737779514  302 InrgkEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDGLNNAVAQKKTNIESLLTRKAALEA 367
Cdd:COG4913   680 L----DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 170-374 3.00e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 3.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514   170 REIQTLTGEIMGRHapgiERGNSKASRLQAGASPADVVNRQVNQLHAELPAEIAAKEAERDAVQA----------DLEKH 239
Cdd:TIGR02168  754 KELTELEAEIEELE----ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanlreRLESL 829

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514   240 QRHLTKAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELERLTLEQAAQQAALDKINRGKEKAQDELSQIKGQ 319
Cdd:TIGR02168  830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK 909

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 737779514   320 QVEARADLAEVETRRAETTSELDGLNNAVAQKKTNI--------ESLLTRKAALEASLQSLRA 374
Cdd:TIGR02168  910 RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseeysltlEEAEALENKIEDDEEEARR 972
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
216-373 1.17e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 47.34  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 216 AELPAEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELE--RLTLEQA 293
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEecRVAAQAH 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 294 AQQA-----ALDKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDGLNNAVAQKKTNIESLLTRKAALEAS 368
Cdd:PRK02224 341 NEEAeslreDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREE 420


                 ....*
gi 737779514 369 LQSLR 373
Cdd:PRK02224 421 RDELR 425
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
237-374 1.41e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  237 EKHQRHltkAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELERLTLEQAAQQAALDKINRGKEKAQDELSQI 316
Cdd:COG4913   259 ELAERY---AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGN 335

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 737779514  317 KGQQVEA-RADLAEVETRRAETTSELDGLNNAVAQKK----TNIESLLTRKAALEASLQSLRA 374
Cdd:COG4913   336 GGDRLEQlEREIERLERELEERERRRARLEALLAALGlplpASAEEFAALRAEAAALLEALEE 398
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
216-373 5.70e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.03  E-value: 5.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 216 AELPAEIAAKEAERDAVQADLEKhqrhltkakadLEKAIaqtgEESAKVETISKRAATYEKRVKTAQAELE--RLTLEQA 293
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLER-----------AEDLV----EAEDRIERLEERREDLEELIAERRETIEekRERAEEL 542

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 294 AQQAA-LDKINRGKEKAQDELsqiKGQQVEARADLAEVETRRAETTSELDGLNnavaqkktNIESLLTRKAALEASLQSL 372
Cdd:PRK02224 543 RERAAeLEAEAEEKREAAAEA---EEEAEEAREEVAELNSKLAELKERIESLE--------RIRTLLAAIADAEDEIERL 611


                 .
gi 737779514 373 R 373
Cdd:PRK02224 612 R 612
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
 217-353 6.15e-05

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 44.99  E-value: 6.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  217 ELPAEIAAKEAER-----DAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELERLTLE 291
Cdd:pfam05262 205 ERESQEDAKRAQQlkeelDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIE 284

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 737779514  292 QAAQQA--ALDKINRGKEKAQDELSQ-IKGQQVEARADLAEVETRRAETTSELDGLNNAVAQKKT 353
Cdd:pfam05262 285 KAQIEIkkNDEEALKAKDHKAFDLKQeSKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPT 349
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 216-313 1.12e-04

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: 43.56  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  216 AELPAEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKRAA-TYEKRVKTAQAELERLTLEQAA 294
Cdd:TIGR04320 257 AALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALqTAQNNLATAQAALANAEARLAK 336

                          90
                  ....*....|....*....
gi 737779514  295 QQAALDKINRGKEKAQDEL 313
Cdd:TIGR04320 337 AKEALANLNADLAKKQAAL 355
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 206-372 1.13e-04

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 43.90  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  206 VVNRQVNQLhAELPAEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQTGEE-----------SAKVETISKRAATY 274
Cdd:pfam19220 182 LSEEQAAEL-AELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQLEEAveahraeraslRMKLEALTARAAAT 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  275 EKRVKTAQAELERLTLEQAAQQAALDKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDGLNNAVAQKKTN 354
Cdd:pfam19220 261 EQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEMLTKALAAKDAA 340

                         170
                  ....*....|....*...
gi 737779514  355 IESLLTRKAALEASLQSL 372
Cdd:pfam19220 341 LERAEERIASLSDRIAEL 358
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 212-374 1.20e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 43.60  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 212 NQLHAELPAEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELERLTLE 291
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 292 QAAQQAALDKINRGKEKAQDE------LSQIKGQQVEARAD-LAEVETRRAETTSELDGLNNAVAQKKTNIESLLTRKAA 364
Cdd:COG4942   99 LEAQKEELAELLRALYRLGRQpplallLSPEDFLDAVRRLQyLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178

                        170
                 ....*....|
gi 737779514 365 LEASLQSLRA 374
Cdd:COG4942  179 LLAELEEERA 188
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
267-374 1.49e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 267 ISKRAATYEKRVKTAQAELERLtleqaAQQAALDKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDGLNN 346
Cdd:COG3206  180 LEEQLPELRKELEEAEAALEEF-----RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254

                         90       100       110
                 ....*....|....*....|....*....|
gi 737779514 347 AVAQKKTN--IESLLTRKAALEASLQSLRA 374
Cdd:COG3206  255 ALPELLQSpvIQQLRAQLAELEAELAELSA 284
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 208-370 2.00e-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: 43.47  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  208 NRQVNQLHAElpaeIAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELER 287
Cdd:TIGR04523 224 KKQNNQLKDN----IEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD 299

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  288 LTLEQAAQ-------------------QAALDKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDGLNNAV 348
Cdd:TIGR04523 300 LNNQKEQDwnkelkselknqekkleeiQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKEN 379

                         170       180
                  ....*....|....*....|..
gi 737779514  349 AQKKTNIESLLTRKAALEASLQ 370
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQ 401
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 226-334 2.12e-04

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 43.40  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  226 EAERDAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELERLTlEQAAQQAALDKINRG 305
Cdd:PRK11448  141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQ-EKAAETSQERKQKRK 219

                          90       100
                  ....*....|....*....|....*....
gi 737779514  306 KekaqdelsqiKGQQVEARADLAEVETRR 334
Cdd:PRK11448  220 E----------ITDQAAKRLELSEEETRI 238
PRK11281 PRK11281
mechanosensitive channel MscK;
194-374 2.57e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 42.98  E-value: 2.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  194 ASRLQAGASPADVVNRQVNQLHAELPAEIAAKEAERDAVQADLEKHQRHLTKakadlekaIAQTGEESAKVEtisKRAAT 273
Cdd:PRK11281   23 SSAFARAASNGDLPTEADVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDK--------IDRQKEETEQLK---QQLAQ 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  274 YEKRVKTAQAELERLTlEQAAQQAALDKINRGKEKAQDELSQIKGQQVEARADLAEVETR---------RAETT-----S 339
Cdd:PRK11281   92 APAKLRQAQAELEALK-DDNDEETRETLSTLSLRQLESRLAQTLDQLQNAQNDLAEYNSQlvslqtqpeRAQAAlyansQ 170

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 737779514  340 ELDGLNNAVAQKKTNIESLL-TRKAALEASLQSLRA 374
Cdd:PRK11281  171 RLQQIRNLLKGGKVGGKALRpSQRVLLQAEQALLNA 206
46 PHA02562
endonuclease subunit; Provisional
 217-374 3.14e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 42.69  E-value: 3.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 217 ELPAEIAAKEAERDAVQADLEKHQRHLTKAKAdleKAIAQTGEESAKVETISKRAATYEKRVKTAQAELERLTLEQAAQQ 296
Cdd:PHA02562 178 ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRK---KNGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPS 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 297 AALDKINRGKEKAQDELSQIKG---------------QQVE-------------------------ARADLAEVETRRAE 336
Cdd:PHA02562 255 AALNKLNTAAAKIKSKIEQFQKvikmyekggvcptctQQISegpdritkikdklkelqhslekldtAIDELEEIMDEFNE 334

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 737779514 337 TTSELDGLNNAVAQKKTNIESLLTRKAALEASLQSLRA 374
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA 372
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
209-373 3.18e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  209 RQVNQLHAELPAEIAAKEAERDAVQADLEKHQRHLTKAKAD-----LEKAIAQTGEESAKVETISKRAATYEKRVKTAQA 283
Cdd:COG4913   620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvasAEREIAELEAELERLDASSDDLAALEEQLEELEA 699

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  284 ELERLTLEQAAQQAALDKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDGLNNAVAQKKTNIESlltRKA 363
Cdd:COG4913   700 ELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE---RID 776

                         170
                  ....*....|
gi 737779514  364 ALEASLQSLR 373
Cdd:COG4913   777 ALRARLNRAE 786
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
201-374 3.45e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 3.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 201 ASPADVVNRqVNQLHAELPAEIAAKEAERDAVQADLEKHQRHLTKAK------ADLEKAIAQTgeESAKVETISKRAATY 274
Cdd:PRK02224 202 KDLHERLNG-LESELAELDEEIERYEEQREQARETRDEADEVLEEHEerreelETLEAEIEDL--RETIAETEREREELA 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 275 EkRVKTAQAELERLTLEQAAQQAALDKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDGLNNAVAQKKTN 354
Cdd:PRK02224 279 E-EVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER 357

                        170       180
                 ....*....|....*....|
gi 737779514 355 IESLLTRKAALEASLQSLRA 374
Cdd:PRK02224 358 AEELREEAAELESELEEARE 377
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 228-341 3.64e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 42.76  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 228 ERDAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKvetiskRAATYEKRVKTAQAELERLTLEQAAQQAALDKINRGKE 307
Cdd:COG0542  405 EIDSKPEELDELERRLEQLEIEKEALKKEQDEASFE------RLAELRDELAELEEELEALKARWEAEKELIEEIQELKE 478

                         90       100       110
                 ....*....|....*....|....*....|....
gi 737779514 308 kaqdELSQIKGQQVEARADLAEVETRRAETTSEL 341
Cdd:COG0542  479 ----ELEQRYGKIPELEKELAELEEELAELAPLL 508
PRK09039 PRK09039
peptidoglycan -binding protein;
205-317 6.69e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.10  E-value: 6.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 205 DVVNRQVNQLH-----------------AELPAEIAAKEAERDAVQADLEKhqrhLTKAKADLEKAIAQTGEESAKVETI 267
Cdd:PRK09039  56 DRLNSQIAELAdllslerqgnqdlqdsvANLRASLSAAEAERSRLQALLAE----LAGAGAAAEGRAGELAQELDSEKQV 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 737779514 268 SKRAATyekRVKTAQAELERLTLEQAAQQAALDkinrgKEKAQDELSQIK 317
Cdd:PRK09039 132 SARALA---QVELLNQQIAALRRQLAALEAALD-----ASEKRDRESQAK 173
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
194-336 7.20e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 7.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 194 ASRLQAGASPADVVNRQVNQLHAELP---AEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKR 270
Cdd:COG4372   30 SEQLRKALFELDKLQEELEQLREELEqarEELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 737779514 271 AATYEKRVKTAQAELERLTLEQAAQQAALDKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAE 336
Cdd:COG4372  110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
220-363 8.67e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 8.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 220 AEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELERLTLEQAAQQAAL 299
Cdd:COG4372   38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737779514 300 DKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDGLNNAVAQKKTNIESLLTRKA 363
Cdd:COG4372  118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEA 181
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 271-370 1.01e-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: 40.90  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 271 AATYEKRVKTAQAELERLTLEQAAQQAALDKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDGLNNAVAQ 350
Cdd:COG4942   15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                         90       100
                 ....*....|....*....|
gi 737779514 351 KKTNIESLLTRKAALEASLQ 370
Cdd:COG4942   95 LRAELEAQKEELAELLRALY 114
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
220-361 1.17e-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: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  220 AEIAAKEAERDAvqADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELERLTLEQAAQQAAL 299
Cdd:COG4913   659 DEIDVASAEREI--AELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL 736

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 737779514  300 DKINRGKEKAQDELSQIKGQQVEARADLAEVetrRAETTSELDGLNNAVAQKKTNIESLLTR 361
Cdd:COG4913   737 EAAEDLARLELRALLEERFAAALGDAVEREL---RENLEERIDALRARLNRAEEELERAMRA 795
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 210-374 1.31e-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: 40.52  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 210 QVNQLHAELPAEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAI--AQTGEESAKVETI-----SKRAATYEKRVKTAQ 282
Cdd:COG4942   66 ALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLraLYRLGRQPPLALLlspedFLDAVRRLQYLKYLA 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 283 AELERLTLEQAAQQAALDKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAETtseLDGLNNAVAQKKTNIESLLTRK 362
Cdd:COG4942  146 PARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEA 222

                        170
                 ....*....|..
gi 737779514 363 AALEASLQSLRA 374
Cdd:COG4942  223 EELEALIARLEA 234
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
222-372 1.88e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 222 IAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELERLTLEQAAQQAALDK 301
Cdd:COG4372   26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 737779514 302 INRGKEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDGLNNAVAQKKTNIESLLTRKAALEASLQSL 372
Cdd:COG4372  106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 264-356 2.34e-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: 39.71  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514  264 VETISKRAATYEKRVKTAQAELERLT--LEQA-----AQQAALDKINRGKEKAQDELSQIKGQQ--------VEARADLA 328
Cdd:TIGR04320 249 IPNPPNSLAALQAKLATAQADLAAAQtaLNTAqaaltSAQTAYAAAQAALATAQKELANAQAQAlqtaqnnlATAQAALA 328

                          90       100
                  ....*....|....*....|....*...
gi 737779514  329 EVETRRAETTSELDGLNNAVAQKKTNIE 356
Cdd:TIGR04320 329 NAEARLAKAKEALANLNADLAKKQAALD 356
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
223-374 2.58e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 223 AAKEAERDAVQADLE-KHQRHLTKAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELERLTLEQAAQQAALDK 301
Cdd:COG4717  348 ELQELLREAEELEEElQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDE 427

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 737779514 302 inrgkEKAQDELSQIKGQQVEARADLAEVETRRAETTSELDGL--NNAVAQKKTNIESLLTRKAALEASLQSLRA 374
Cdd:COG4717  428 -----EELEEELEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELKAELRELAEEWAALKL 497
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 197-374 4.06e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 197 LQAGASPADVVNRQVNQLHAELPAEIAAKEAERDAVQADLEKHQRHLTKAKADLEKA---IAQTGEESAKVET-ISKRAA 272
Cdd:COG3883    7 AAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALqaeIDKLQAEIAEAEAeIEERRE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 273 TYEKRVKTAQ----------------------AELERLTLEQAAQQAALDKINRGKEKAQDELSQIKGQQVEARADLAEV 330
Cdd:COG3883   87 ELGERARALYrsggsvsyldvllgsesfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 737779514 331 ETRRAETTSELDGLNNAVAQKKTNIESLLTRKAALEASLQSLRA 374
Cdd:COG3883  167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 216-374 5.00e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.00  E-value: 5.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514   216 AELPAEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKRAATYEKRVKTAQAELERL------T 289
Cdd:pfam01576  232 AELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALkteledT 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514   290 LEQAAQQAALdkinrgKEKAQDELSQIK-GQQVEARADLAEVETRRAETTSELDGLNNAVAQKKTNIESLLTRKAALEAS 368
Cdd:pfam01576  312 LDTTAAQQEL------RSKREQEVTELKkALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESE 385


                   ....*.
gi 737779514   369 LQSLRA 374
Cdd:pfam01576  386 NAELQA 391
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
195-367 5.42e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 5.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 195 SRLQAGASPADVVNRQVNQLHaELPAEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQtgeesAKVETISKRAATY 274
Cdd:COG4717   78 EELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALE-----AELAELPERLEEL 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 275 EKRVKtaqaELERLTLEQAAQQAALDKINRGKEKAQDELSQIKGQQVE-ARADLAEVETRRAETTSELDGLNNAVAQKKT 353
Cdd:COG4717  152 EERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELEELEE 227

                        170
                 ....*....|....
gi 737779514 354 NIESLLTRKAALEA 367
Cdd:COG4717  228 ELEQLENELEAAAL 241
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
216-333 5.94e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 38.32  E-value: 5.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 216 AELPAEIAAKEAERDAVQADLEKHQRHLTKAKADLEKAIAQTgEESAKVETISKRAATyEKRVKTAQAELER---LTLEQ 292
Cdd:COG2268  208 AERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK-KAEERREAETARAEA-EAAYEIAEANAERevqRQLEI 285

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 737779514 293 AAQQAALDKINRGKEKAQDELSQIKGQQVEARADLAEVETR 333
Cdd:COG2268  286 AEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAE 326
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
220-336 6.16e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 38.32  E-value: 6.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 220 AEIAAKEAERDAVQADLEKHQR-HLTKAKADLEKAIAQTGEESAKVEtisKRAATYEKRVKTAQAELERLTLEQA--AQQ 296
Cdd:COG2268  201 ARIAEAEAERETEIAIAQANREaEEAELEQEREIETARIAEAEAELA---KKKAEERREAETARAEAEAAYEIAEanAER 277

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 737779514 297 AALDKINRGKEKAQDELSQIKGQQVEARADLAEVETRRAE 336
Cdd:COG2268  278 EVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAE 317
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 230-373 8.92e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 37.73  E-value: 8.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 737779514 230 DAVQADLEKHQRHLTKAKADLEKAIAQTGEESAKVETISKR---------AATYEKRVKTAQAELERLTLEQAAQ-QAAL 299
Cdd:cd22656  124 DDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKAlkdlltdegGAIARKEIKDLQKELEKLNEEYAAKlKAKI 203

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 737779514 300 DKINRGKEKAQDELSQIKgqqvEARADLAEVETrraettsELDGLNNAVAQKKTNIESLLTRKAALEASLQSLR 373
Cdd:cd22656  204 DELKALIADDEAKLAAAL----RLIADLTAADT-------DLDNLLALIGPAIPALEKLQGAWQAIATDLDSLK 266
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH