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Conserved domains on  [gi|564372498|ref|XP_006246640|]
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nuclear distribution protein nudE-like 1 isoform X3 [Rattus norvegicus]

Protein Classification

SPEC and NUDE_C domain-containing protein( domain architecture ID 10522326)

SPEC and NUDE_C domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NUDE_C pfam04880
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ...
 135-309 1.90e-55

NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved region of the NUDE proteins. NUDE proteins are involved in nuclear migration.


:

Pssm-ID: 461464 [Multi-domain]  Cd Length: 169  Bit Score: 178.06  E-value: 1.90e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  135 SLEDFEQRLNQAIERNAFLESEL----DEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSP---TLDCEKMD 207
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKLRNLLMRSPSTPslqTLEIFDRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  208 SAVQASlslpATPVG-KGTENSFPSpkAIPNGFGTSPLTPSARISAlnivgDLLRKVGALESKLAACRNFAKDQASRKSY 286
Cdd:pfam04880  81 PAVQAV----SSPVIaTPPEKSFNS--LRTGSETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNASRRG 149

                         170       180
                  ....*....|....*....|...
gi 564372498  287 vpgSVNCGVMNSNGPECPRSGRA 309
Cdd:pfam04880 150 ---NSRSLYGSRPPTKFAHSRHT 169
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-195 4.32e-10

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 4.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  27 KQSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAqsykQVSVLEDDLSQ 103
Cdd:COG1196  273 RLELEELELELEEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEEELAELEEELEELEE----ELEELEEELEE 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498 104 TRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAV 183
Cdd:COG1196  349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428

                        170
                 ....*....|..
gi 564372498 184 RERQQEVTRKSA 195
Cdd:COG1196  429 ALAELEEEEEEE 440
 
Name Accession Description Interval E-value
NUDE_C pfam04880
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ...
 135-309 1.90e-55

NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved region of the NUDE proteins. NUDE proteins are involved in nuclear migration.


Pssm-ID: 461464 [Multi-domain]  Cd Length: 169  Bit Score: 178.06  E-value: 1.90e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  135 SLEDFEQRLNQAIERNAFLESEL----DEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSP---TLDCEKMD 207
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKLRNLLMRSPSTPslqTLEIFDRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  208 SAVQASlslpATPVG-KGTENSFPSpkAIPNGFGTSPLTPSARISAlnivgDLLRKVGALESKLAACRNFAKDQASRKSY 286
Cdd:pfam04880  81 PAVQAV----SSPVIaTPPEKSFNS--LRTGSETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNASRRG 149

                         170       180
                  ....*....|....*....|...
gi 564372498  287 vpgSVNCGVMNSNGPECPRSGRA 309
Cdd:pfam04880 150 ---NSRSLYGSRPPTKFAHSRHT 169
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-195 4.32e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 4.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  27 KQSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAqsykQVSVLEDDLSQ 103
Cdd:COG1196  273 RLELEELELELEEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEEELAELEEELEELEE----ELEELEEELEE 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498 104 TRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAV 183
Cdd:COG1196  349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428

                        170
                 ....*....|..
gi 564372498 184 RERQQEVTRKSA 195
Cdd:COG1196  429 ALAELEEEEEEE 440
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 24-195 1.66e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 1.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    24 LKYKQSFQEARDELVEFQEGSRELEAELEA---QLVQAEQRNRDLQADNQRLKYEVEALKEklehQYAQSYKQVSVLEDD 100
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAElrkELEELEEELEQLRKELEELSRQISALRK----DLARLEAEVEQLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   101 LSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESllvSVQRLKDEARDLRQE 180
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANLRER 825

                          170
                   ....*....|....*
gi 564372498   181 LAVRERQQEVTRKSA 195
Cdd:TIGR02168  826 LESLERRIAATERRL 840
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 31-258 1.84e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.14  E-value: 1.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYaQSYKQVSVLE------------ 98
Cdd:COG3883   40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY-RSGGSVSYLDvllgsesfsdfl 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  99 DDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLR 178
Cdd:COG3883  119 DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498 179 QELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENSFPSPKAIPNGFGTSPLTPSARISALNIVGD 258
Cdd:COG3883  199 AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAA 278
PRK09039 PRK09039
peptidoglycan -binding protein;
22-149 7.44e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 43.80  E-value: 7.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  22 LSLKyKQSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKekleHQYAQSYKQVSVLE 98
Cdd:PRK09039  69 LSLE-RQGNQDLQDSVANLRASLSAAEAErsrLQALLAELAGAGAAAEGRAGELAQELDSEK----QVSARALAQVELLN 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564372498  99 DDLSqtrAIKEQLHKyvreLEQANDDLERAKRATIVSLEDFEQRLNQAIER 149
Cdd:PRK09039 144 QQIA---ALRRQLAA----LEAALDASEKRDRESQAKIADLGRRLNVALAQ 187
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 27-192 9.70e-05

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 44.06  E-value: 9.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    27 KQSFQEARDEL----VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKE-----KLEHQYA-QSYKQV-- 94
Cdd:pfam12128  645 RTALKNARLDLrrlfDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEeqkeqKREARTEkQAYWQVve 724

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    95 ---SVLEDDLSQTRAIKEQLHK---------YVREL------EQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESE 156
Cdd:pfam12128  725 galDAQLALLKAAIAARRSGAKaelkaletwYKRDLaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQET 804

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 564372498   157 -LDEKESLLVSVQRLKDEARDLRQELAvreRQQEVTR 192
Cdd:pfam12128  805 wLQRRPRLATQLSNIERAISELQQQLA---RLIADTK 838
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
 143-189 6.89e-04

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 40.73  E-value: 6.89e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 564372498 143 LNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQE 189
Cdd:PRK13922  71 LFDLREENEELKKELLELESRLQELEQLEAENARLRELLNLKESLDY 117
 
Name Accession Description Interval E-value
NUDE_C pfam04880
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ...
 135-309 1.90e-55

NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved region of the NUDE proteins. NUDE proteins are involved in nuclear migration.


Pssm-ID: 461464 [Multi-domain]  Cd Length: 169  Bit Score: 178.06  E-value: 1.90e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  135 SLEDFEQRLNQAIERNAFLESEL----DEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSP---TLDCEKMD 207
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKLRNLLMRSPSTPslqTLEIFDRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  208 SAVQASlslpATPVG-KGTENSFPSpkAIPNGFGTSPLTPSARISAlnivgDLLRKVGALESKLAACRNFAKDQASRKSY 286
Cdd:pfam04880  81 PAVQAV----SSPVIaTPPEKSFNS--LRTGSETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNASRRG 149

                         170       180
                  ....*....|....*....|...
gi 564372498  287 vpgSVNCGVMNSNGPECPRSGRA 309
Cdd:pfam04880 150 ---NSRSLYGSRPPTKFAHSRHT 169
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 27-195 4.32e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 4.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  27 KQSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAqsykQVSVLEDDLSQ 103
Cdd:COG1196  273 RLELEELELELEEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEEELAELEEELEELEE----ELEELEEELEE 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498 104 TRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAV 183
Cdd:COG1196  349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428

                        170
                 ....*....|..
gi 564372498 184 RERQQEVTRKSA 195
Cdd:COG1196  429 ALAELEEEEEEE 440
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
27-188 1.22e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.46  E-value: 1.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   27 KQSFQEARDELVEFQEGSRELEaELEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQS-YKQVSVLEDDLS 102
Cdd:COG4913   270 RLAELEYLRAALRLWFAQRRLE-LLEAELEELRAELARLEAELERLEARLDALREEldeLEAQIRGNgGDRLEQLEREIE 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  103 QTRAIKEQLhkyVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKE----SLLVSVQRLKDEARDLR 178
Cdd:COG4913   349 RLERELEER---ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEealaEAEAALRDLRRELRELE 425

                         170
                  ....*....|
gi 564372498  179 QELAVRERQQ 188
Cdd:COG4913   426 AEIASLERRK 435
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 24-195 1.66e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 1.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    24 LKYKQSFQEARDELVEFQEGSRELEAELEA---QLVQAEQRNRDLQADNQRLKYEVEALKEklehQYAQSYKQVSVLEDD 100
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAElrkELEELEEELEQLRKELEELSRQISALRK----DLARLEAEVEQLEER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   101 LSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESllvSVQRLKDEARDLRQE 180
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANLRER 825

                          170
                   ....*....|....*
gi 564372498   181 LAVRERQQEVTRKSA 195
Cdd:TIGR02168  826 LESLERRIAATERRL 840
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 13-192 1.74e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  13 KEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQ 89
Cdd:COG1196  220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyeLLAELAR 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  90 SYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQR 169
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                        170       180
                 ....*....|....*....|....*...
gi 564372498 170 LKDEARD-----LRQELAVRERQQEVTR 192
Cdd:COG1196  380 ELEELAEelleaLRAAAELAAQLEELEE 407
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 27-193 5.37e-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: 54.29  E-value: 5.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    27 KQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRA 106
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALREALDELRA 810

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   107 IKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLvsvQRLKDEARDLRQELAVRER 186
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI---EELESELEALLNERASLEE 887


                   ....*..
gi 564372498   187 QQEVTRK 193
Cdd:TIGR02168  888 ALALLRS 894
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
27-193 1.38e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  27 KQSFQEARDELVEFQEGSRELEaELEAQLVQAEQRNRDLQADNQRLKYEVEAL-----KEKLEHQYAQSYKQVSVLEDDL 101
Cdd:COG4717   77 EEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLLQLLplyqeLEALEAELAELPERLEELEERL 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498 102 SQTRAIKEQLHKYVRELEQANDDLERAKRATivsLEDFEQRLNQAIERNAFLESELDEKESLLvsvQRLKDEARDLRQEL 181
Cdd:COG4717  156 EELRELEEELEELEAELAELQEELEELLEQL---SLATEEELQDLAEELEELQQRLAELEEEL---EEAQEELEELEEEL 229

                        170
                 ....*....|..
gi 564372498 182 AVRERQQEVTRK 193
Cdd:COG4717  230 EQLENELEAAAL 241
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
45-192 1.58e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.00  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   45 RELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHqyAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDD 124
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREA--LQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  125 LERAKR---ATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDL------------RQELAVRERQQE 189
Cdd:COG4913   687 LAALEEqleELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelralleerFAAALGDAVERE 766


                  ...
gi 564372498  190 VTR 192
Cdd:COG4913   767 LRE 769
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 31-258 1.84e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.14  E-value: 1.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYaQSYKQVSVLE------------ 98
Cdd:COG3883   40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY-RSGGSVSYLDvllgsesfsdfl 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  99 DDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLR 178
Cdd:COG3883  119 DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498 179 QELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENSFPSPKAIPNGFGTSPLTPSARISALNIVGD 258
Cdd:COG3883  199 AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAA 278
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 31-189 1.99e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 1.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQ 110
Cdd:COG1196  333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA-EAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564372498 111 LhkyVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQE 189
Cdd:COG1196  412 L---LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 10-199 5.31e-07

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: 50.53  E-value: 5.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  10 SSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEA---ELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQ 86
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  87 YAQSYK--QVSVLE-----DDLSQT-------RAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAF 152
Cdd:COG4942  110 LRALYRlgRQPPLAlllspEDFLDAvrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564372498 153 LESELDEKESLLVSVQR-----------LKDEARDLRQELAVRERQQEVTRKSAPSSP 199
Cdd:COG4942  190 LEALKAERQKLLARLEKelaelaaelaeLQQEAEELEALIARLEAEAAAAAERTPAAG 247
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 8-202 8.15e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.84  E-value: 8.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498     8 DFSSLKEETAYWkELSLKYKqsfqEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQY 87
Cdd:TIGR02169  215 ALLKEKREYEGY-ELLKEKE----ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    88 AQSYKQVSVLEDDLSQTRAIKEQLHKYVRELE--QANDDLERakRATIVSLEDFEQRLNQAIERNAFLESELDEK----E 161
Cdd:TIGR02169  290 LRVKEKIGELEAEIASLERSIAEKERELEDAEerLAKLEAEI--DKLLAEIEELEREIEEERKRRDKLTEEYAELkeelE 367

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 564372498   162 SLLVSVQRLKDEARDLRQELA-VRERQQEVTRKSAPSSPTLD 202
Cdd:TIGR02169  368 DLRAELEEVDKEFAETRDELKdYREKLEKLKREINELKRELD 409
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 28-195 1.28e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  28 QSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQT 104
Cdd:COG1196  302 QDIARLEERRRELEERLEELEEElaeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498 105 RAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVR 184
Cdd:COG1196  382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                        170
                 ....*....|.
gi 564372498 185 ERQQEVTRKSA 195
Cdd:COG1196  462 LELLAELLEEA 472
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 20-193 1.81e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 1.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    20 KELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQaeqrnrdLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLED 99
Cdd:TIGR02168  227 LALLVLRLEELREELEELQEELKEAEEELEELTAELQE-------LEEKLEELRLEVSELEEEIEELQKELYALANEISR 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   100 DLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDF---EQRLNQAIERNAFLESELDEKESLLV----SVQRLKD 172
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELaelEEKLEELKEELESLEAELEELEAELEelesRLEELEE 379

                          170       180
                   ....*....|....*....|.
gi 564372498   173 EARDLRQELAVRERQQEVTRK 193
Cdd:TIGR02168  380 QLETLRSKVAQLELQIASLNN 400
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 39-195 2.27e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 2.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  39 EFQEGSRELEAELeaQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVREL 118
Cdd:COG1196  217 ELKEELKELEAEL--LLLKLRELEAELEELEAELE-ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564372498 119 EQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSA 195
Cdd:COG1196  294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 4-177 2.66e-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: 2.66e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498     4 EDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQ---LVQAEQRNRDLQADNQRLKYEVEALK 80
Cdd:TIGR02168  334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLrskVAQLELQIASLNNEIERLEARLERLE 413

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    81 --------EKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAF 152
Cdd:TIGR02168  414 drrerlqqEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493

                          170       180
                   ....*....|....*....|....*
gi 564372498   153 LESELDEKESLLVSVQRLKDEARDL 177
Cdd:TIGR02168  494 LERLQENLEGFSEGVKALLKNQSGL 518
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 25-189 1.02e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    25 KYKQSFQEARDELVEFQEGSRELEAELEA---QLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDL 101
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   102 SQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDF---EQRLNQAIERNAFLESELDEKESllvSVQRLKDEARDLR 178
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERaslEEALALLRSELEELSEELRELES---KRSELRRELEELR 921

                          170
                   ....*....|..
gi 564372498   179 QELA-VRERQQE 189
Cdd:TIGR02168  922 EKLAqLELRLEG 933
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 10-195 1.15e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 1.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    10 SSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQ------ADNQRLKYEVEALKEKL 83
Cdd:TIGR02169  691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSsleqeiENVKSELKELEARIEEL 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    84 EHQYAQSYKQVSVLEDDLSQTRaikeqlhkyVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESL 163
Cdd:TIGR02169  771 EEDLHKLEEALNDLEARLSHSR---------IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841

                          170       180       190
                   ....*....|....*....|....*....|....
gi 564372498   164 LVSVQRLKDEARDLRQEL--AVRERQQEVTRKSA 195
Cdd:TIGR02169  842 RIDLKEQIKSIEKEIENLngKKEELEEELEELEA 875
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 31-196 1.64e-05

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 45.30  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEq 110
Cdd:COG1579   13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-DLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498 111 LHKYVRELEQA---NDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKEsllvsvQRLKDEARDLRQELAVRERQ 187
Cdd:COG1579   91 YEALQKEIESLkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK------AELDEELAELEAELEELEAE 164


                 ....*....
gi 564372498 188 QEVTRKSAP 196
Cdd:COG1579  165 REELAAKIP 173
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 31-182 2.43e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 2.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALK---EKLEHQYAQSYKQVSVLEDDLSQTRAI 107
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEeliEELESELEALLNERASLEEALALLRSE 895

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   108 KEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLV------------SVQRLKDEAR 175
Cdd:TIGR02168  896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLeeaealenkiedDEEEARRRLK 975


                   ....*..
gi 564372498   176 DLRQELA 182
Cdd:TIGR02168  976 RLENKIK 982
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 30-195 6.26e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 6.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    30 FQEARDELVEFQE---GSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQ---YAQSYKQVSVLEDDLSQ 103
Cdd:TIGR02168  276 VSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEELKEELES 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   104 TRAIKEQLHKYVRELEQANDDLERAkrativsLEDFEQRLNQAIERNAFLESELdekESLLVSVQRLKDEARDLRQELAV 183
Cdd:TIGR02168  356 LEAELEELEAELEELESRLEELEEQ-------LETLRSKVAQLELQIASLNNEI---ERLEARLERLEDRRERLQQEIEE 425

                          170
                   ....*....|..
gi 564372498   184 RERQQEVTRKSA 195
Cdd:TIGR02168  426 LLKKLEEAELKE 437
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 12-189 6.48e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 6.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    12 LKEETAYWKELSLKYKQSFQEARDELVEFqegsRELEAELEAQLVQAEQrnrdlQADNQRLKYevealkEKLEHQYAQSY 91
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLEAELEEL----EAELEELESRLEELEE-----QLETLRSKV------AQLELQIASLN 399

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    92 KQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVS-----LEDFEQRLNQAIERNAFLESELDEKESLLVS 166
Cdd:TIGR02168  400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEeleeeLEELQEELERLEEALEELREELEEAEQALDA 479

                          170       180
                   ....*....|....*....|...
gi 564372498   167 vqrLKDEARDLRQELAVRERQQE 189
Cdd:TIGR02168  480 ---AERELAQLQARLDSLERLQE 499
PRK09039 PRK09039
peptidoglycan -binding protein;
22-149 7.44e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 43.80  E-value: 7.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  22 LSLKyKQSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKekleHQYAQSYKQVSVLE 98
Cdd:PRK09039  69 LSLE-RQGNQDLQDSVANLRASLSAAEAErsrLQALLAELAGAGAAAEGRAGELAQELDSEK----QVSARALAQVELLN 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564372498  99 DDLSqtrAIKEQLHKyvreLEQANDDLERAKRATIVSLEDFEQRLNQAIER 149
Cdd:PRK09039 144 QQIA---ALRRQLAA----LEAALDASEKRDRESQAKIADLGRRLNVALAQ 187
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
50-192 7.90e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 7.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  50 ELEAQLVQAEQRNRDLQADNQRLKY---EVEALKEKLEH--QYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQAndd 124
Cdd:COG4717   75 ELEEELKEAEEKEEEYAELQEELEEleeELEELEAELEElrEELEKLEKLLQLLPLYQELEALEAELAELPERLEEL--- 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498 125 leRAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLV--SVQRLKDEARDLRQELAVRERQQEVTR 192
Cdd:COG4717  152 --EERLEELRELEEELEELEAELAELQEELEELLEQLSLATeeELQDLAEELEELQQRLAELEEELEEAQ 219
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 27-192 9.70e-05

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 44.06  E-value: 9.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    27 KQSFQEARDEL----VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKE-----KLEHQYA-QSYKQV-- 94
Cdd:pfam12128  645 RTALKNARLDLrrlfDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEeqkeqKREARTEkQAYWQVve 724

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    95 ---SVLEDDLSQTRAIKEQLHK---------YVREL------EQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESE 156
Cdd:pfam12128  725 galDAQLALLKAAIAARRSGAKaelkaletwYKRDLaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQET 804

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 564372498   157 -LDEKESLLVSVQRLKDEARDLRQELAvreRQQEVTR 192
Cdd:pfam12128  805 wLQRRPRLATQLSNIERAISELQQQLA---RLIADTK 838
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 27-183 1.35e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 43.79  E-value: 1.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   27 KQSFQEARDELVEFQEGSRELEAELEA-----QLVQAEQRnrdLQADNQRLKYEVEALKEKLEHQ---YAQSYKQVSVLE 98
Cdd:COG3096   305 QYRLVEMARELEELSARESDLEQDYQAasdhlNLVQTALR---QQEKIERYQEDLEELTERLEEQeevVEEAAEQLAEAE 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   99 DDLSQTRA----IKEQLHKYVRELE----------QANDDLERAKR---ATIVSLEDFEQRLnqaiernafleSELDEKE 161
Cdd:COG3096   382 ARLEAAEEevdsLKSQLADYQQALDvqqtraiqyqQAVQALEKARAlcgLPDLTPENAEDYL-----------AAFRAKE 450

                         170       180
                  ....*....|....*....|..
gi 564372498  162 sllvsvQRLKDEARDLRQELAV 183
Cdd:COG3096   451 ------QQATEEVLELEQKLSV 466
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 12-225 1.53e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 1.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    12 LKEETAYWKElslkYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALK----------E 81
Cdd:TIGR02169  838 LQEQRIDLKE----QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELErkieeleaqiE 913

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    82 KLEHQYAQSYKQVSVLEDDLSQTRAIK-------------EQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIE 148
Cdd:TIGR02169  914 KKRKRLSELKAKLEALEEELSEIEDPKgedeeipeeelslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE 993

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564372498   149 RNAFLESELDEKESLLVSVQRLKDEARdLRQELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGT 225
Cdd:TIGR02169  994 KRAKLEEERKAILERIEEYEKKKREVF-MEAFEAINENFNEIFAELSGGTGELILENPDDPFAGGLELSAKPKGKPV 1069
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 24-196 1.81e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    24 LKYKQSFQEARDELVEFQEGSRELE---AELEAQLV----QAE--QRNRDLQADNQRLK-----YEVEALKEKLEH---Q 86
Cdd:TIGR02168  168 SKYKERRKETERKLERTRENLDRLEdilNELERQLKslerQAEkaERYKELKAELRELElallvLRLEELREELEElqeE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    87 YAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVS 166
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327

                          170       180       190
                   ....*....|....*....|....*....|
gi 564372498   167 VQRLKDEARDLRQELAVRERQQEVTRKSAP 196
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLE 357
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
25-198 2.63e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 2.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  25 KYKQSFQEARDELVEFQEGSRELEAELEA-----QLVQAEQRNRDLQADNQRLKYEVEALKEKLEH-------------- 85
Cdd:COG3206  186 ELRKELEEAEAALEEFRQKNGLVDLSEEAklllqQLSELESQLAEARAELAEAEARLAALRAQLGSgpdalpellqspvi 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  86 -QYAQSYKQVSVLEDDLSQT--------RAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESE 156
Cdd:COG3206  266 qQLRAQLAELEAELAELSARytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE 345

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564372498 157 LDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSS 198
Cdd:COG3206  346 LPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
 143-189 6.89e-04

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 40.73  E-value: 6.89e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 564372498 143 LNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQE 189
Cdd:PRK13922  71 LFDLREENEELKKELLELESRLQELEQLEAENARLRELLNLKESLDY 117
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 41-194 8.15e-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: 40.90  E-value: 8.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  41 QEGSRELEAELEaQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRA----IKEQLHKYVR 116
Cdd:COG4942   19 ADAAAEAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAelaeLEKEIAELRA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498 117 ELEQANDDLERAKRAT-----------IVSLEDFEQ--RLNQAIER-NAFLESELDEKESLLVSVQRLKDEARDLRQELA 182
Cdd:COG4942   98 ELEAQKEELAELLRALyrlgrqpplalLLSPEDFLDavRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELE 177

                        170
                 ....*....|..
gi 564372498 183 VRERQQEVTRKS 194
Cdd:COG4942  178 ALLAELEEERAA 189
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
38-187 8.64e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 8.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  38 VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALK--EKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYV 115
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDriERLEERREDLEELIAERRETIEEKRERAEELRERA 546

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498 116 RELE--------QANDDLERA--KRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLkdeaRDLRQELAVRE 185
Cdd:PRK02224 547 AELEaeaeekreAAAEAEEEAeeAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERL----REKREALAELN 622


                 ..
gi 564372498 186 RQ 187
Cdd:PRK02224 623 DE 624
mukB PRK04863
chromosome partition protein MukB;
35-189 9.03e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.10  E-value: 9.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   35 DELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQrlkyevealkeklehQYAQSYKQVSVLEDDLSQTRAIK------ 108
Cdd:PRK04863  438 DNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHS---------------QFEQAYQLVRKIAGEVSRSEAWDvarell 502

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  109 -------------EQLHKYVRELEQANDDLERAKRAtivsLEDFEQRLNQAIERNAFLESELDEKESLLVSvqrLKDEAR 175
Cdd:PRK04863  503 rrlreqrhlaeqlQQLRMRLSELEQRLRQQQRAERL----LAEFCKRLGKNLDDEDELEQLQEELEARLES---LSESVS 575

                         170
                  ....*....|....
gi 564372498  176 DLRQELAVRERQQE 189
Cdd:PRK04863  576 EARERRMALRQQLE 589
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 31-148 9.79e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.97  E-value: 9.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLqadnQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQT--RAIK 108
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEA----EALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqQAIK 580

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 564372498 109 E------QLHKYVRELEQANDDLERAKRativsLEDFEQRLNQAIE 148
Cdd:PRK00409 581 EakkeadEIIKELRQLQKGGYASVKAHE-----LIEARKRLNKANE 621
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
31-182 1.01e-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: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   31 QEARDELVEFQEGSRELEA------ELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQ--------SYKQVSV 96
Cdd:COG4913   671 AELEAELERLDASSDDLAAleeqleELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaedlaRLELRAL 750

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   97 LEDDLSQ----------TRAIKEQLHKYVRELEQANDDLERAKR--------------ATIVSLEDFEQRLNQAIE---- 148
Cdd:COG4913   751 LEERFAAalgdaverelRENLEERIDALRARLNRAEEELERAMRafnrewpaetadldADLESLPEYLALLDRLEEdglp 830

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 564372498  149 ------RNAFLESELDEKESLLvsvQRLKDEARDLRQELA 182
Cdd:COG4913   831 eyeerfKELLNENSIEFVADLL---SKLRRAIREIKERID 867
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
20-193 1.12e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  20 KELSLKYKQSFQEARDELVEFQEGSRELEAEL---------EAQLVQAEQRNRDLQADNQRLK-YEVEALK------EKL 83
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELrelekvlkkESELIKLKELAEQLKELEEKLKkYNLEELEkkaeeyEKL 530

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  84 EHQYAQSYKQVSVLEDDL-------SQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESE 156
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELekleelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDA 610

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 564372498 157 LDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRK 193
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
49-190 1.20e-03

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 40.03  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  49 AELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKlehqyaqsykqvsvleddlsqtRAIKEQLHKYVRELEQANDDLERA 128
Cdd:COG1566   79 TDLQAALAQAEAQLAAAEAQLARLEAELGAEAEI----------------------AAAEAQLAAAQAQLDLAQRELERY 136

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564372498 129 KRAT---IVSLEDFEQRLNQAIErnafLESELDEKESLLVSVQRLKDEARDLRQ-ELAVRERQQEV 190
Cdd:COG1566  137 QALYkkgAVSQQELDEARAALDA----AQAQLEAAQAQLAQAQAGLREEEELAAaQAQVAQAEAAL 198
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
12-190 1.36e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  12 LKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQlvqaeQRNRDLQADNQRLKYEVEALKEKLEH------ 85
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-----ERIRTLLAAIADAEDEIERLREKREAlaelnd 623

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  86 ----QYAQSYKQVSVLEDD-----LSQTRAIKEQLHKYVRELEQANDDLERAK---RATIVSLEDFEQRLNQAIERNAFL 153
Cdd:PRK02224 624 erreRLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERddlQAEIGAVENELEELEELRERREAL 703

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 564372498 154 ESELDEKESLLVSVQRLKDEARDLRQELavreRQQEV 190
Cdd:PRK02224 704 ENRVEALEALYDEAEELESMYGDLRAEL----RQRNV 736
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
32-180 1.39e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  32 EARDELV---EFQEGSRE----LEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQSYKQVSVLEDDL 101
Cdd:PRK02224 293 EERDDLLaeaGLDDADAEaveaRREELEDRDEELRDRLEECRVAAQAHNEEAESLREDaddLEERAEELREEAAELESEL 372

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564372498 102 SQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQE 180
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEA 451
PRK12705 PRK12705
hypothetical protein; Provisional
 25-189 1.65e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.08  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  25 KYKQSFQEARDELVEFQEGSREL--EAELEAQLVQAEQRNRDLQADNQRlkyevealKEKLEHQYAQSYKQvsvleddls 102
Cdd:PRK12705  27 KRQRLAKEAERILQEAQKEAEEKleAALLEAKELLLRERNQQRQEARRE--------REELQREEERLVQK--------- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498 103 qtraiKEQLHKYVRELEQANDDLERAKRAtivsledFEQRLNQAIERNAFLESELDEKESLLVSVQR---LKDEARDLRQ 179
Cdd:PRK12705  90 -----EEQLDARAEKLDNLENQLEEREKA-------LSARELELEELEKQLDNELYRVAGLTPEQARkllLKLLDAELEE 157

                        170
                 ....*....|
gi 564372498 180 ELAVRERQQE 189
Cdd:PRK12705 158 EKAQRVKKIE 167
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 32-212 1.66e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    32 EARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQSYKQVSVLEDDLSQTR 105
Cdd:TIGR02169  788 LSHSRIPEIQAELSKLEEEvsrIEARLREIEQKLNRLTLEKEYLEKEIQELQEQridLKEQIKSIEKEIENLNGKKEELE 867

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   106 AIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQaiernafLESELDEKESLLvsvQRLKDEARDLRQELAVRE 185
Cdd:TIGR02169  868 EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-------LEAQIEKKRKRL---SELKAKLEALEEELSEIE 937

                          170       180
                   ....*....|....*....|....*..
gi 564372498   186 RqqEVTRKSAPSSPTLDCEKMDSAVQA 212
Cdd:TIGR02169  938 D--PKGEDEEIPEEELSLEDVQAELQR 962
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 41-196 1.73e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.32  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   41 QEGSRELEAELEAQLVQAEQRNRDLQadnQRLkyeveALKEKLEHQYAQSYKQVSVLEDDLSQTRA---IKEQLHKY--- 114
Cdd:COG3096   436 PENAEDYLAAFRAKEQQATEEVLELE---QKL-----SVADAARRQFEKAYELVCKIAGEVERSQAwqtARELLRRYrsq 507

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  115 -------------VRELEQANDDLERAKRativSLEDFEQRLNQAIERNAFLESELDE----KESLLVSVQRLKDEARDL 177
Cdd:COG3096   508 qalaqrlqqlraqLAELEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAEleaqLEELEEQAAEAVEQRSEL 583

                         170       180
                  ....*....|....*....|
gi 564372498  178 RQEL-AVRERQQEVTRKsAP 196
Cdd:COG3096   584 RQQLeQLRARIKELAAR-AP 602
FtsB COG2919
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
49-84 1.92e-03

Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442163 [Multi-domain]  Cd Length: 96  Bit Score: 37.17  E-value: 1.92e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 564372498  49 AELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLE 84
Cdd:COG2919   32 RELRQEIAELEAENAKLKARNAELEAEVADLKDGPD 67
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 44-200 2.38e-03

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: 39.33  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   44 SRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYkqvsvleddlSQTRAIKEQLHKYVRELEQAND 123
Cdd:pfam00529  56 YQAALDSAEAQLAKAQAQVARLQAELDRLQ-ALESELAISRQDYDGAT----------AQLRAAQAAVKAAQAQLAQAQI 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  124 DLERAK-RATI--VSLEDF-EQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELA-----VRERQQEVTRKS 194
Cdd:pfam00529 125 DLARRRvLAPIggISRESLvTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSgaqlqIAEAEAELKLAK 204


                  ....*.
gi 564372498  195 APSSPT 200
Cdd:pfam00529 205 LDLERT 210
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 12-183 2.88e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 39.32  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   12 LKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSY 91
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKE 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   92 KQVSVLeddLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDfeqrLNQAIERNAFLESELdekESLLVSVQRLK 171
Cdd:pfam05483 240 KQVSLL---LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDEN----LKELIEKKDHLTKEL---EDIKMSLQRSM 309

                         170
                  ....*....|..
gi 564372498  172 DEARDLRQELAV 183
Cdd:pfam05483 310 STQKALEEDLQI 321
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 12-211 2.92e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.57  E-value: 2.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    12 LKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELE-----AELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQ 86
Cdd:TIGR00618  251 AQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaAPLAAHIKAVTQIEQQAQRIHTELQ-SKMRSRAKLLMK 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    87 YAQSYKQvsvlEDDLSQTRAIKEQLHKYVRELEQANDD----LERAKRATIVS--LEDFEQRLNQAIERNAFLESELDEK 160
Cdd:TIGR00618  330 RAAHVKQ----QSSIEEQRRLLQTLHSQEIHIRDAHEVatsiREISCQQHTLTqhIHTLQQQKTTLTQKLQSLCKELDIL 405

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 564372498   161 ESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAP-----SSPTLDCEKMDSAVQ 211
Cdd:TIGR00618  406 QREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAElcaaaITCTAQCEKLEKIHL 461
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
 29-154 3.40e-03

LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.


Pssm-ID: 462869 [Multi-domain]  Cd Length: 303  Bit Score: 38.52  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   29 SFQEARDELVEFQEGSREleaeleAQLVQAeqrnrdlQADNQR--LKYEVEALKEKLEHqyaqsykqvsvLEDDLSQTRa 106
Cdd:pfam09738  87 SLRDIKHELKEVEEKYRK------AMISNA-------QLDNEKsnLMYQVDLLKDKLEE-----------MEESLAELQ- 141

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 564372498  107 ikeqlhkyvRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLE 154
Cdd:pfam09738 142 ---------RELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIE 180
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
27-193 3.74e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 3.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  27 KQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRA 106
Cdd:COG4372   30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE-QLEEELEELNEQLQAAQAELAQAQEELESLQE 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498 107 IKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRER 186
Cdd:COG4372  109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188


                 ....*..
gi 564372498 187 QQEVTRK 193
Cdd:COG4372  189 LKEANRN 195
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 45-147 3.77e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 37.96  E-value: 3.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   45 RELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQyaQSYKQvsvledDLSQTRAIKEQLHKYVRELEQANDD 124
Cdd:pfam13851  39 KKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENY--EKDKQ------SLKNLKARLKVLEKELKDLKWEHEV 110

                          90       100
                  ....*....|....*....|...
gi 564372498  125 LERAKRATIVSLEDFEQRLNQAI 147
Cdd:pfam13851 111 LEQRFEKVERERDELYDKFEAAI 133
mukB PRK04863
chromosome partition protein MukB;
6-184 4.65e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.78  E-value: 4.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    6 IPDFSSLKEETaywkelslkYKQSFQEARDELVEFQEGSR----------ELEAEL------EAQLVQAEQRNRDLQADN 69
Cdd:PRK04863  881 LPRLNLLADET---------LADRVEEIREQLDEAEEAKRfvqqhgnalaQLEPIVsvlqsdPEQFEQLKQDYQQAQQTQ 951

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   70 QRLKYEVEALKEKLEHQYAQSYKQVsvlEDDLSQTRAIKEQLHkyvRELEQANDDLERAKRAtivsLEDFEQRLNQAIER 149
Cdd:PRK04863  952 RDAKQQAFALTEVVQRRAHFSYEDA---AEMLAKNSDLNEKLR---QRLEQAEQERTRAREQ----LRQAQAQLAQYNQV 1021

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 564372498  150 NAFLESELDEKEsllvsvQRLKDEARDLrQELAVR 184
Cdd:PRK04863 1022 LASLKSSYDAKR------QMLQELKQEL-QDLGVP 1049
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
31-193 4.99e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   31 QEARDELVEFQEGSRELEAELEA--QLVQAEQRNRDLQADNQRLKYEVEALK--------EKLEHQYAQSYKQVSVLEDD 100
Cdd:COG4913   231 VEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRlwfaqrrlELLEAELEELRAELARLEAE 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  101 LSQTRAIKEQLHKYVRELEQAN--------DDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQR--- 169
Cdd:COG4913   311 LERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAeaa 390

                         170       180
                  ....*....|....*....|....*
gi 564372498  170 -LKDEARDLRQELAVRERQQEVTRK 193
Cdd:COG4913   391 aLLEALEEELEALEEALAEAEAALR 415
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 13-190 5.29e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 38.40  E-value: 5.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  13 KEETAYWKELSLKYKQSFQEARdELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEklEHQYAQSYK 92
Cdd:COG5185  301 YTKSIDIKKATESLEEQLAAAE-AEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVG--EVELSKSSE 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  93 QvsvLEDDLSQTRAIKEQLHKYVRELEQANDD----LERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQ 168
Cdd:COG5185  378 E---LDSFKDTIESTKESLDEIPQNQRGYAQEilatLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVM 454

                        170       180
                 ....*....|....*....|..
gi 564372498 169 RLKDEARDLRQELAVRERQQEV 190
Cdd:COG5185  455 READEESQSRLEEAYDEINRSV 476
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 41-195 6.95e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 37.95  E-value: 6.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   41 QEGSRELEAELEAQLVQAEQRNRDlqadnqrlKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQ 120
Cdd:pfam07888  37 EECLQERAELLQAQEAANRQREKE--------KERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564372498  121 ANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLvsvQRLKDeardlRQELAVRERQQEVTRKSA 195
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETEL---ERMKE-----RAKKAGAQRKEEEAERKQ 175
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 32-195 7.91e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 38.03  E-value: 7.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498    32 EARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQL 111
Cdd:pfam02463  153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   112 hKYVRELEQANDDLERAKRATIVSledfEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVT 191
Cdd:pfam02463  233 -KLNEERIDLLQELLRDEQEEIES----SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307


                   ....
gi 564372498   192 RKSA 195
Cdd:pfam02463  308 RKVD 311
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
49-194 8.01e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.07  E-value: 8.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  49 AELEAQLVQAEQRNRDLQADNQRLKYEVEALkeklehqyaQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERA 128
Cdd:COG3206  185 PELRKELEEAEAALEEFRQKNGLVDLSEEAK---------LLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDA 255

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498 129 KRATIVSledfeQRLNQAIERNAFLESELDEKESLLV----SVQRLKDEARDLRQELAVRERQQEVTRKS 194
Cdd:COG3206  256 LPELLQS-----PVIQQLRAQLAELEAELAELSARYTpnhpDVIALRAQIAALRAQLQQEAQRILASLEA 320
PRK12704 PRK12704
phosphodiesterase; Provisional
 13-173 8.43e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.84  E-value: 8.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  13 KEEtayWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKY---EVEALKEKLEHQYAq 89
Cdd:PRK12704  63 KEE---IHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQkqqELEKKEEELEELIE- 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  90 syKQVSVLED--DLSQTRAiKEQLhkyvreLEQANDDLERAKRATIvsledfeqrlnQAIERNAFLESELDEKESLLVSV 167
Cdd:PRK12704 139 --EQLQELERisGLTAEEA-KEIL------LEKVEEEARHEAAVLI-----------KEIEEEAKEEADKKAKEILAQAI 198


                 ....*.
gi 564372498 168 QRLKDE 173
Cdd:PRK12704 199 QRCAAD 204
PilN COG3166
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
139-189 8.58e-03

Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];


Pssm-ID: 442399 [Multi-domain]  Cd Length: 185  Bit Score: 36.87  E-value: 8.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564372498 139 FEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQE 189
Cdd:COG3166   43 LQGQIAQQQARNAALQQEIAKLDKQIAEIKELKKQKAELLARLQVIEQLQQ 93
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 10-181 8.65e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 37.80  E-value: 8.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   10 SSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEaqlvQAEQRNRDLQADNQRLKYEVEALKEkLEHQYAQ 89
Cdd:pfam05557 107 SCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKAS----EAEQLRQNLEKQQSSLAEAEQRIKE-LEFEIQS 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   90 SykqvsvlEDDLSQTRAIKEQLHKYvreleqanDDLERAKRAtivsLEDFEQRLNQAIERNAFLESELDEKESLLVSVQR 169
Cdd:pfam05557 182 Q-------EQDSEIVKNSKSELARI--------PELEKELER----LREHNKHLNENIENKLLLKEEVEDLKRKLEREEK 242

                         170
                  ....*....|..
gi 564372498  170 LKDEARDLRQEL 181
Cdd:pfam05557 243 YREEAATLELEK 254
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 27-149 8.76e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.21  E-value: 8.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498  27 KQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKE--KLEHQYAQSYKQVSVLEDDLSQT 104
Cdd:COG1579   37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG-NVRNNKEyeALQKEIESLKRRISDLEDEILEL 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 564372498 105 RAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIER 149
Cdd:COG1579  116 MERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 49-196 9.45e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 36.47  E-value: 9.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   49 AELEAQLVQAEQR-----NRDLQADNQRLKYEVEALKEKLEhQYAQSYKQvsVLEDDLSQTRAikeQLHKYVREL-EQAN 122
Cdd:pfam01442  14 EELQEQLGPVAQElvdrlEKETEALRERLQKDLEEVRAKLE-PYLEELQA--KLGQNVEELRQ---RLEPYTEELrKRLN 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564372498  123 DDLERAKRATIVSLEDFEQRLNQAIER-NAFLESELDE-KESLLVSVQRLKDEARDLRQEL--AVRERQQEVTRKSAP 196
Cdd:pfam01442  88 ADAEELQEKLAPYGEELRERLEQNVDAlRARLAPYAEElRQKLAERLEELKESLAPYAEEVqaQLSQRLQELREKLEP 165
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 38-181 9.84e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 38.01  E-value: 9.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564372498   38 VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEhQYAQSYKQVSVLEDDLSQTRaikeqlhkyVRE 117
Cdd:COG3096   828 VAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQ-LLNKLLPQANLLADETLADR---------LEE 897

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564372498  118 LEQANDDLERAKRativSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQEL 181
Cdd:COG3096   898 LREELDAAQEAQA----FIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQI 957
 
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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