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Conserved domains on  [gi|1720368068|ref|XP_030102302|]
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nuclear distribution protein nudE-like 1 isoform X1 [Mus musculus]

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 1.18e-53

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: 174.21  E-value: 1.18e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 135 SLEDFEQRLNQAIERNAFLESEL----DEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSP---TLDCEKMD 207
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKLRNLLMRSPSTPslqTLEIFDRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 208 SAVQASlslpATPVG-KGTENSFPSpkAIPNGFGTSPLTPSARISAlnivgDLLRKVGALESKLAACRNFAKDQASRKSY 286
Cdd:pfam04880  81 PAVQAV----SSPVIaTPPEKSFNS--LRTGSETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNASRRG 149
                         170       180
                  ....*....|....*....|...
gi 1720368068 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 9.81e-11

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: 63.03  E-value: 9.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  27 KQSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAqsykQVSVLEDDLSQ 103
Cdd:COG1196   273 RLELEELELELEEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEEELAELEEELEELEE----ELEELEEELEE 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 104 TRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAV 183
Cdd:COG1196   349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
                         170
                  ....*....|..
gi 1720368068 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 1.18e-53

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: 174.21  E-value: 1.18e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 135 SLEDFEQRLNQAIERNAFLESEL----DEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSP---TLDCEKMD 207
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKLRNLLMRSPSTPslqTLEIFDRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 208 SAVQASlslpATPVG-KGTENSFPSpkAIPNGFGTSPLTPSARISAlnivgDLLRKVGALESKLAACRNFAKDQASRKSY 286
Cdd:pfam04880  81 PAVQAV----SSPVIaTPPEKSFNS--LRTGSETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNASRRG 149
                         170       180
                  ....*....|....*....|...
gi 1720368068 287 vpgSVNCGVMNSNGPECPRSGRA 309
Cdd:pfam04880 150 ---NSRSLYGSRPPTKFAHSRHT 169
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
27-195 9.81e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 9.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  27 KQSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAqsykQVSVLEDDLSQ 103
Cdd:COG1196   273 RLELEELELELEEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEEELAELEEELEELEE----ELEELEEELEE 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 104 TRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAV 183
Cdd:COG1196   349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
                         170
                  ....*....|..
gi 1720368068 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 2.65e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.53  E-value: 2.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   24 LKYKQSFQEARDELVEFQEGSRELEAELEA---QLVQAEQRNRDLQADNQRLKYEVEALKEklehQYAQSYKQVSVLEDD 100
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAElrkELEELEEELEQLRKELEELSRQISALRK----DLARLEAEVEQLEER 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  101 LSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESllvSVQRLKDEARDLRQE 180
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANLRER 825
                          170
                   ....*....|....*
gi 1720368068  181 LAVRERQQEVTRKSA 195
Cdd:TIGR02168  826 LESLERRIAATERRL 840
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
31-258 5.16e-08

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.07  E-value: 5.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYaQSYKQVSVLE------------ 98
Cdd:COG3883    40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY-RSGGSVSYLDvllgsesfsdfl 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  99 DDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLR 178
Cdd:COG3883   119 DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 179 QELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENSFPSPKAIPNGFGTSPLTPSARISALNIVGD 258
Cdd:COG3883   199 AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAA 278
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
27-192 1.74e-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: 46.76  E-value: 1.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   27 KQSFQEARDEL----VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKE-----KLEHQYA-QSYKQV-- 94
Cdd:pfam12128  645 RTALKNARLDLrrlfDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEeqkeqKREARTEkQAYWQVve 724
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   95 ---SVLEDDLSQTRAIKEQLHK---------YVREL------EQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESE 156
Cdd:pfam12128  725 galDAQLALLKAAIAARRSGAKaelkaletwYKRDLaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQET 804
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1720368068  157 -LDEKESLLVSVQRLKDEARDLRQELAvreRQQEVTR 192
Cdd:pfam12128  805 wLQRRPRLATQLSNIERAISELQQQLA---RLIADTK 838
PRK09039 PRK09039
peptidoglycan -binding protein;
22-149 5.08e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 44.57  E-value: 5.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  22 LSLKyKQSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKekleHQYAQSYKQVSVLE 98
Cdd:PRK09039   69 LSLE-RQGNQDLQDSVANLRASLSAAEAErsrLQALLAELAGAGAAAEGRAGELAQELDSEK----QVSARALAQVELLN 143
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720368068  99 DDLSqtrAIKEQLHKyvreLEQANDDLERAKRATIVSLEDFEQRLNQAIER 149
Cdd:PRK09039  144 QQIA---ALRRQLAA----LEAALDASEKRDRESQAKIADLGRRLNVALAQ 187
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
143-189 6.59e-04

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 40.73  E-value: 6.59e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1720368068 143 LNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQE 189
Cdd:PRK13922   71 LFDLREENEELKKELLELESRLQELEQLEAENARLRELLNLKESLDY 117
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
36-185 9.24e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 37.04  E-value: 9.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  36 ELVEFQEGSRELEAELEA--QLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQyAQSYKQVSVLEDDLSQTRAI-KEQLH 112
Cdd:cd00176     1 KLQQFLRDADELEAWLSEkeELLSSTDYGDDLESVEALLK-KHEALEAELAAH-EERVEALNELGEQLIEEGHPdAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 113 KYVRELEQANDDLERAkrativsLEDFEQRLNQAIERNAF------LESELDEKESLLVS---------VQRLKDEARDL 177
Cdd:cd00176    79 ERLEELNQRWEELREL-------AEERRQRLEEALDLQQFfrdaddLEQWLEEKEAALASedlgkdlesVEELLKKHKEL 151

                  ....*...
gi 1720368068 178 RQELAVRE 185
Cdd:cd00176   152 EEELEAHE 159
 
Name Accession Description Interval E-value
NUDE_C pfam04880
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ...
135-309 1.18e-53

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: 174.21  E-value: 1.18e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 135 SLEDFEQRLNQAIERNAFLESEL----DEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSP---TLDCEKMD 207
Cdd:pfam04880   1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKLRNLLMRSPSTPslqTLEIFDRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 208 SAVQASlslpATPVG-KGTENSFPSpkAIPNGFGTSPLTPSARISAlnivgDLLRKVGALESKLAACRNFAKDQASRKSY 286
Cdd:pfam04880  81 PAVQAV----SSPVIaTPPEKSFNS--LRTGSETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNASRRG 149
                         170       180
                  ....*....|....*....|...
gi 1720368068 287 vpgSVNCGVMNSNGPECPRSGRA 309
Cdd:pfam04880 150 ---NSRSLYGSRPPTKFAHSRHT 169
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
27-195 9.81e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.03  E-value: 9.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  27 KQSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAqsykQVSVLEDDLSQ 103
Cdd:COG1196   273 RLELEELELELEEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEEELAELEEELEELEE----ELEELEEELEE 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 104 TRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAV 183
Cdd:COG1196   349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
                         170
                  ....*....|..
gi 1720368068 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 2.65e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.53  E-value: 2.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   24 LKYKQSFQEARDELVEFQEGSRELEAELEA---QLVQAEQRNRDLQADNQRLKYEVEALKEklehQYAQSYKQVSVLEDD 100
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAElrkELEELEEELEQLRKELEELSRQISALRK----DLARLEAEVEQLEER 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  101 LSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESllvSVQRLKDEARDLRQE 180
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANLRER 825
                          170
                   ....*....|....*
gi 1720368068  181 LAVRERQQEVTRKSA 195
Cdd:TIGR02168  826 LESLERRIAATERRL 840
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
27-188 2.90e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.39  E-value: 2.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   27 KQSFQEARDELVEFQEGSRELEaELEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQS-YKQVSVLEDDLS 102
Cdd:COG4913    270 RLAELEYLRAALRLWFAQRRLE-LLEAELEELRAELARLEAELERLEARLDALREEldeLEAQIRGNgGDRLEQLEREIE 348
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  103 QTRAIKEQLhkyVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKE----SLLVSVQRLKDEARDLR 178
Cdd:COG4913    349 RLERELEER---ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEealaEAEAALRDLRRELRELE 425
                          170
                   ....*....|
gi 1720368068  179 QELAVRERQQ 188
Cdd:COG4913    426 AEIASLERRK 435
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
13-192 4.51e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 4.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  13 KEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQ 89
Cdd:COG1196   220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyeLLAELAR 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  90 SYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQR 169
Cdd:COG1196   300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
                         170       180
                  ....*....|....*....|....*...
gi 1720368068 170 LKDEARD-----LRQELAVRERQQEVTR 192
Cdd:COG1196   380 ELEELAEelleaLRAAAELAAQLEELEE 407
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
27-193 7.78e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.08  E-value: 7.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  27 KQSFQEARDELVEFQEGSRELEaELEAQLVQAEQRNRDLQADNQRLKYEVEAL-----KEKLEHQYAQSYKQVSVLEDDL 101
Cdd:COG4717    77 EEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLLQLLplyqeLEALEAELAELPERLEELEERL 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 102 SQTRAIKEQLHKYVRELEQANDDLERAKRATivsLEDFEQRLNQAIERNAFLESELDEKESLLvsvQRLKDEARDLRQEL 181
Cdd:COG4717   156 EELRELEEELEELEAELAELQEELEELLEQL---SLATEEELQDLAEELEELQQRLAELEEEL---EEAQEELEELEEEL 229
                         170
                  ....*....|..
gi 1720368068 182 AVRERQQEVTRK 193
Cdd:COG4717   230 EQLENELEAAAL 241
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
27-193 1.07e-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: 56.60  E-value: 1.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   27 KQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRA 106
Cdd:TIGR02168  732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALREALDELRA 810
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  107 IKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLvsvQRLKDEARDLRQELAVRER 186
Cdd:TIGR02168  811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI---EELESELEALLNERASLEE 887

                   ....*..
gi 1720368068  187 QQEVTRK 193
Cdd:TIGR02168  888 ALALLRS 894
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
45-192 4.99e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.54  E-value: 4.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   45 RELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHqyAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDD 124
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREA--LQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD 686
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  125 LERAKR---ATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDL------------RQELAVRERQQE 189
Cdd:COG4913    687 LAALEEqleELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelralleerFAAALGDAVERE 766

                   ...
gi 1720368068  190 VTR 192
Cdd:COG4913    767 LRE 769
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
31-258 5.16e-08

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 54.07  E-value: 5.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYaQSYKQVSVLE------------ 98
Cdd:COG3883    40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY-RSGGSVSYLDvllgsesfsdfl 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  99 DDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLR 178
Cdd:COG3883   119 DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 179 QELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENSFPSPKAIPNGFGTSPLTPSARISALNIVGD 258
Cdd:COG3883   199 AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAA 278
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
31-189 5.64e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 5.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQ 110
Cdd:COG1196   333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA-EAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720368068 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, ...
10-219 9.69e-08

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: 53.23  E-value: 9.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  10 SSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEA---ELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQ 86
Cdd:COG4942    30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  87 YAQSYK--QVSVLE-----DDLSQT-------RAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAF 152
Cdd:COG4942   110 LRALYRlgRQPPLAlllspEDFLDAvrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720368068 153 LESELDEKESLLVSVQR-----------LKDEARDLRQELAVRERQQEVTRKSAPSSPTldcekmdSAVQASLSLPAT 219
Cdd:COG4942   190 LEALKAERQKLLARLEKelaelaaelaeLQQEAEELEALIARLEAEAAAAAERTPAAGF-------AALKGKLPWPVS 260
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
8-202 1.04e-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: 53.53  E-value: 1.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068    8 DFSSLKEETAYWkELSLKYKqsfqEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQY 87
Cdd:TIGR02169  215 ALLKEKREYEGY-ELLKEKE----ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   88 AQSYKQVSVLEDDLSQTRAIKEQLHKYVRELE--QANDDLERakRATIVSLEDFEQRLNQAIERNAFLESELDEK----E 161
Cdd:TIGR02169  290 LRVKEKIGELEAEIASLERSIAEKERELEDAEerLAKLEAEI--DKLLAEIEELEREIEEERKRRDKLTEEYAELkeelE 367
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1720368068  162 SLLVSVQRLKDEARDLRQELA-VRERQQEVTRKSAPSSPTLD 202
Cdd:TIGR02169  368 DLRAELEEVDKEFAETRDELKdYREKLEKLKREINELKRELD 409
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
20-193 3.32e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 3.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   20 KELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEhqyaQSYKQVSVLEd 99
Cdd:TIGR02168  227 LALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY----ALANEISRLE- 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  100 dlSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDF---EQRLNQAIERNAFLESELDEKESLLV----SVQRLKD 172
Cdd:TIGR02168  302 --QQKQILRERLANLERQLEELEAQLEELESKLDELAEELaelEEKLEELKEELESLEAELEELEAELEelesRLEELEE 379
                          170       180
                   ....*....|....*....|.
gi 1720368068  173 EARDLRQELAVRERQQEVTRK 193
Cdd:TIGR02168  380 QLETLRSKVAQLELQIASLNN 400
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
31-195 4.26e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 4.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  31 QEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAI 107
Cdd:COG1196   305 ARLEERRRELEERLEELEEElaeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 108 KEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQ 187
Cdd:COG1196   385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464

                  ....*...
gi 1720368068 188 QEVTRKSA 195
Cdd:COG1196   465 LAELLEEA 472
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4-177 5.68e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.21  E-value: 5.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068    4 EDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQ---LVQAEQRNRDLQADNQRLKYEVEALK 80
Cdd:TIGR02168  334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLrskVAQLELQIASLNNEIERLEARLERLE 413
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   81 --------EKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAF 152
Cdd:TIGR02168  414 drrerlqqEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
                          170       180
                   ....*....|....*....|....*
gi 1720368068  153 LESELDEKESLLVSVQRLKDEARDL 177
Cdd:TIGR02168  494 LERLQENLEGFSEGVKALLKNQSGL 518
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
39-195 6.74e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 6.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  39 EFQEGSRELEAELeaQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVREL 118
Cdd:COG1196   217 ELKEELKELEAEL--LLLKLRELEAELEELEAELE-ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720368068 119 EQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSA 195
Cdd:COG1196   294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
31-196 1.40e-06

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: 48.77  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEq 110
Cdd:COG1579    13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-DLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 111 LHKYVRELEQA---NDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKEsllvsvQRLKDEARDLRQELAVRERQ 187
Cdd:COG1579    91 YEALQKEIESLkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK------AELDEELAELEAELEELEAE 164

                  ....*....
gi 1720368068 188 QEVTRKSAP 196
Cdd:COG1579   165 REELAAKIP 173
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
20-192 1.71e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  20 KELSLKYKQSFQEARDELVEFQEGSRELEA----------------ELEAQLVQAEQRNRDLQADNQRLKY--------- 74
Cdd:COG4717    53 KEADELFKPQGRKPELNLKELKELEEELKEaeekeeeyaelqeeleELEEELEELEAELEELREELEKLEKllqllplyq 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  75 EVEALKEKLEH---QYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATivsLEDFEQRLNQAIERNA 151
Cdd:COG4717   133 ELEALEAELAElpeRLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDLAEELEELQQRLA 209
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720368068 152 FLESELDEKESllvSVQRLKDEARDLRQELAVRERQQEVTR 192
Cdd:COG4717   210 ELEEELEEAQE---ELEELEEELEQLENELEAAALEERLKE 247
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
25-189 1.80e-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: 1.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   25 KYKQSFQEARDELVEFQEGSRELEAELEA---QLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDL 101
Cdd:TIGR02168  765 ELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  102 SQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDF---EQRLNQAIERNAFLESELDEKESllvSVQRLKDEARDLR 178
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERaslEEALALLRSELEELSEELRELES---KRSELRRELEELR 921
                          170
                   ....*....|..
gi 1720368068  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 2.14e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 2.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   10 SSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQ------ADNQRLKYEVEALKEKL 83
Cdd:TIGR02169  691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSsleqeiENVKSELKELEARIEEL 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   84 EHQYAQSYKQVSVLEDDLSQTRaikeqlhkyVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESL 163
Cdd:TIGR02169  771 EEDLHKLEEALNDLEARLSHSR---------IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1720368068  164 LVSVQRLKDEARDLRQEL--AVRERQQEVTRKSA 195
Cdd:TIGR02169  842 RIDLKEQIKSIEKEIENLngKKEELEEELEELEA 875
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
12-182 5.20e-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: 48.51  E-value: 5.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   12 LKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELE---AELEAQLVQAEQRNRDLQADNQRLKYEVEALK---EKLEH 85
Cdd:TIGR02168  794 LKEELKALREALDELRAELTLLNEEAANLRERLESLErriAATERRLEDLEEQIEELSEDIESLAAEIEELEeliEELES 873
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   86 QYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLV 165
Cdd:TIGR02168  874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL 953
                          170       180
                   ....*....|....*....|....*....
gi 1720368068  166 ------------SVQRLKDEARDLRQELA 182
Cdd:TIGR02168  954 eeaealenkiedDEEEARRRLKRLENKIK 982
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
12-189 9.27e-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: 47.36  E-value: 9.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   12 LKEETAYWKELSLKYKQSFQEARDELVEFqegsRELEAELEAQLVQAEQrnrdlQADNQRLKYevealkEKLEHQYAQSY 91
Cdd:TIGR02168  335 LAEELAELEEKLEELKEELESLEAELEEL----EAELEELESRLEELEE-----QLETLRSKV------AQLELQIASLN 399
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   92 KQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVS-----LEDFEQRLNQAIERNAFLESELDEKESLLVS 166
Cdd:TIGR02168  400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEeleeeLEELQEELERLEEALEELREELEEAEQALDA 479
                          170       180
                   ....*....|....*....|...
gi 1720368068  167 vqrLKDEARDLRQELAVRERQQE 189
Cdd:TIGR02168  480 ---AERELAQLQARLDSLERLQE 499
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
30-195 1.13e-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: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   30 FQEARDELVEFQE---GSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQ---YAQSYKQVSVLEDDLSQ 103
Cdd:TIGR02168  276 VSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEELKEELES 355
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  104 TRAIKEQLHKYVRELEQANDDLERAkrativsLEDFEQRLNQAIERNAFLESELdekESLLVSVQRLKDEARDLRQELAV 183
Cdd:TIGR02168  356 LEAELEELEAELEELESRLEELEEQ-------LETLRSKVAQLELQIASLNNEI---ERLEARLERLEDRRERLQQEIEE 425
                          170
                   ....*....|..
gi 1720368068  184 RERQQEVTRKSA 195
Cdd:TIGR02168  426 LLKKLEEAELKE 437
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
27-192 1.74e-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: 46.76  E-value: 1.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   27 KQSFQEARDEL----VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKE-----KLEHQYA-QSYKQV-- 94
Cdd:pfam12128  645 RTALKNARLDLrrlfDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEeqkeqKREARTEkQAYWQVve 724
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   95 ---SVLEDDLSQTRAIKEQLHK---------YVREL------EQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESE 156
Cdd:pfam12128  725 galDAQLALLKAAIAARRSGAKaelkaletwYKRDLaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQET 804
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1720368068  157 -LDEKESLLVSVQRLKDEARDLRQELAvreRQQEVTR 192
Cdd:pfam12128  805 wLQRRPRLATQLSNIERAISELQQQLA---RLIADTK 838
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
12-225 2.43e-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: 46.21  E-value: 2.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   12 LKEETAYWKElslkYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALK----------E 81
Cdd:TIGR02169  838 LQEQRIDLKE----QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELErkieeleaqiE 913
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   82 KLEHQYAQSYKQVSVLEDDLSQTRAIK-------------EQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIE 148
Cdd:TIGR02169  914 KKRKRLSELKAKLEALEEELSEIEDPKgedeeipeeelslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE 993
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720368068  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 3.19e-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: 45.82  E-value: 3.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   24 LKYKQSFQEARDELVEFQEGSRELE---AELEAQLV----QAE--QRNRDLQADNQRLK-----YEVEALKEKLEH---Q 86
Cdd:TIGR02168  168 SKYKERRKETERKLERTRENLDRLEdilNELERQLKslerQAEkaERYKELKAELRELElallvLRLEELREELEElqeE 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   87 YAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVS 166
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
                          170       180       190
                   ....*....|....*....|....*....|
gi 1720368068  167 VQRLKDEARDLRQELAVRERQQEVTRKSAP 196
Cdd:TIGR02168  328 LESKLDELAEELAELEEKLEELKEELESLE 357
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
27-183 3.50e-05

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: 45.71  E-value: 3.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   27 KQSFQEARDELVEFQEGSRELEAELEA-----QLVQAEQRnrdLQADNQRLKYEVEALKEKLEHQ---YAQSYKQVSVLE 98
Cdd:COG3096    305 QYRLVEMARELEELSARESDLEQDYQAasdhlNLVQTALR---QQEKIERYQEDLEELTERLEEQeevVEEAAEQLAEAE 381
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   99 DDLSQTRA----IKEQLHKYVRELE----------QANDDLERAKR---ATIVSLEDFEQRLnqaiernafleSELDEKE 161
Cdd:COG3096    382 ARLEAAEEevdsLKSQLADYQQALDvqqtraiqyqQAVQALEKARAlcgLPDLTPENAEDYL-----------AAFRAKE 450
                          170       180
                   ....*....|....*....|..
gi 1720368068  162 sllvsvQRLKDEARDLRQELAV 183
Cdd:COG3096    451 ------QQATEEVLELEQKLSV 466
PRK09039 PRK09039
peptidoglycan -binding protein;
22-149 5.08e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 44.57  E-value: 5.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  22 LSLKyKQSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKekleHQYAQSYKQVSVLE 98
Cdd:PRK09039   69 LSLE-RQGNQDLQDSVANLRASLSAAEAErsrLQALLAELAGAGAAAEGRAGELAQELDSEK----QVSARALAQVELLN 143
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720368068  99 DDLSqtrAIKEQLHKyvreLEQANDDLERAKRATIVSLEDFEQRLNQAIER 149
Cdd:PRK09039  144 QQIA---ALRRQLAA----LEAALDASEKRDRESQAKIADLGRRLNVALAQ 187
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
27-193 8.54e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.12  E-value: 8.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  27 KQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRA 106
Cdd:COG4372    30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE-QLEEELEELNEQLQAAQAELAQAQEELESLQE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 107 IKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRER 186
Cdd:COG4372   109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188

                  ....*..
gi 1720368068 187 QQEVTRK 193
Cdd:COG4372   189 LKEANRN 195
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
25-198 1.32e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  25 KYKQSFQEARDELVEFQE--GSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEH-------------- 85
Cdd:COG3206   186 ELRKELEEAEAALEEFRQknGLVDLSEEaklLLQQLSELESQLAEARAELAEAEARLAALRAQLGSgpdalpellqspvi 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  86 -QYAQSYKQVSVLEDDLSQT--------RAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERnafLESE 156
Cdd:COG3206   266 qQLRAQLAELEAELAELSARytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQ---LEAR 342
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1720368068 157 LD---EKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSS 198
Cdd:COG3206   343 LAelpELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
20-193 1.45e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  20 KELSLKYKQSFQEARDELVEFQEGSRELEAEL---------EAQLVQAEQRNRDLQADNQRLK-YEVEALK------EKL 83
Cdd:PRK03918  451 KELLEEYTAELKRIEKELKEIEEKERKLRKELrelekvlkkESELIKLKELAEQLKELEEKLKkYNLEELEkkaeeyEKL 530
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  84 EHQYAQSYKQVSVLEDDL-------SQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESE 156
Cdd:PRK03918  531 KEKLIKLKGEIKSLKKELekleelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDA 610
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1720368068 157 LDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRK 193
Cdd:PRK03918  611 EKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
12-211 1.85e-04

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: 43.42  E-value: 1.85e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   12 LKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELE-----AELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQ 86
Cdd:TIGR00618  251 AQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaAPLAAHIKAVTQIEQQAQRIHTELQ-SKMRSRAKLLMK 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   87 YAQSYKQvsvlEDDLSQTRAIKEQLHKYVRELEQANDD----LERAKRATIVS--LEDFEQRLNQAIERNAFLESELDEK 160
Cdd:TIGR00618  330 RAAHVKQ----QSSIEEQRRLLQTLHSQEIHIRDAHEVatsiREISCQQHTLTqhIHTLQQQKTTLTQKLQSLCKELDIL 405
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720368068  161 ESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAP-----SSPTLDCEKMDSAVQ 211
Cdd:TIGR00618  406 QREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAElcaaaITCTAQCEKLEKIHL 461
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
41-194 1.89e-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: 42.83  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  41 QEGSRELEAELEaQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRA----IKEQLHKYVR 116
Cdd:COG4942    19 ADAAAEAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAelaeLEKEIAELRA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 117 ELEQANDDLERAKRAT-----------IVSLEDFEQ--RLNQAIER-NAFLESELDEKESLLVSVQRLKDEARDLRQELA 182
Cdd:COG4942    98 ELEAQKEELAELLRALyrlgrqpplalLLSPEDFLDavRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELE 177
                         170
                  ....*....|..
gi 1720368068 183 VRERQQEVTRKS 194
Cdd:COG4942   178 ALLAELEEERAA 189
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
31-182 2.31e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 2.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   31 QEARDELVEFQEGSRELEA------ELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQ--------SYKQVSV 96
Cdd:COG4913    671 AELEAELERLDASSDDLAAleeqleELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaedlaRLELRAL 750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   97 LEDDLSQ----------TRAIKEQLHKYVRELEQANDDLERAKR--------------ATIVSLEDFEQRLNQAIE---- 148
Cdd:COG4913    751 LEERFAAalgdaverelRENLEERIDALRARLNRAEEELERAMRafnrewpaetadldADLESLPEYLALLDRLEEdglp 830
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1720368068  149 ------RNAFLESELDEKESLLvsvQRLKDEARDLRQELA 182
Cdd:COG4913    831 eyeerfKELLNENSIEFVADLL---SKLRRAIREIKERID 867
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
38-187 2.56e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  38 VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALK--EKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYV 115
Cdd:PRK02224  467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDriERLEERREDLEELIAERRETIEEKRERAEELRERA 546
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 116 RELE--------QANDDLERA--KRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLkdeaRDLRQELAVRE 185
Cdd:PRK02224  547 AELEaeaeekreAAAEAEEEAeeAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERL----REKREALAELN 622

                  ..
gi 1720368068 186 RQ 187
Cdd:PRK02224  623 DE 624
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
12-183 2.93e-04

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: 42.79  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  12 LKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSY 91
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKE 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  92 KQVSVLeddLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDfeqrLNQAIERNAFLESELdekESLLVSVQRLK 171
Cdd:pfam05483 240 KQVSLL---LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDEN----LKELIEKKDHLTKEL---EDIKMSLQRSM 309
                         170
                  ....*....|..
gi 1720368068 172 DEARDLRQELAV 183
Cdd:pfam05483 310 STQKALEEDLQI 321
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
32-212 3.00e-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: 42.75  E-value: 3.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   32 EARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQSYKQVSVLEDDLSQTR 105
Cdd:TIGR02169  788 LSHSRIPEIQAELSKLEEEvsrIEARLREIEQKLNRLTLEKEYLEKEIQELQEQridLKEQIKSIEKEIENLNGKKEELE 867
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  106 AIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQaiernafLESELDEKESLLvsvQRLKDEARDLRQELAVRE 185
Cdd:TIGR02169  868 EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-------LEAQIEKKRKRL---SELKAKLEALEEELSEIE 937
                          170       180
                   ....*....|....*....|....*..
gi 1720368068  186 RqqEVTRKSAPSSPTLDCEKMDSAVQA 212
Cdd:TIGR02169  938 D--PKGEDEEIPEEELSLEDVQAELQR 962
mukB PRK04863
chromosome partition protein MukB;
35-189 3.14e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.64  E-value: 3.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   35 DELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQrlkyevealkeklehQYAQSYKQVSVLEDDLSQTRAIK------ 108
Cdd:PRK04863   438 DNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHS---------------QFEQAYQLVRKIAGEVSRSEAWDvarell 502
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  109 -------------EQLHKYVRELEQANDDLERAKRAtivsLEDFEQRLNQAIERNAFLESELDEKESLLVSvqrLKDEAR 175
Cdd:PRK04863   503 rrlreqrhlaeqlQQLRMRLSELEQRLRQQQRAERL----LAEFCKRLGKNLDDEDELEQLQEELEARLES---LSESVS 575
                          170
                   ....*....|....
gi 1720368068  176 DLRQELAVRERQQE 189
Cdd:PRK04863   576 EARERRMALRQQLE 589
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
45-161 3.52e-04

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: 41.05  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  45 RELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQyaQSYKQvsvledDLSQTRAIKEQLHKYVRELEQANDD 124
Cdd:pfam13851  39 KKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENY--EKDKQ------SLKNLKARLKVLEKELKDLKWEHEV 110
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720368068 125 LERAKRATIVSLEDFEQRLNQAIE--------RNAFLES-------ELDEKE 161
Cdd:pfam13851 111 LEQRFEKVERERDELYDKFEAAIQdvqqktglKNLLLEKklqalgeTLEKKE 162
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
6-190 3.62e-04

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: 42.25  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   6 IPDFSSLKEETA-YWKELSLK-----YKQSFQEARdELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEAL 79
Cdd:COG5185   288 IKQFENTKEKIAeYTKSIDIKkatesLEEQLAAAE-AEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENI 366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  80 KEklEHQYAQSYKQvsvLEDDLSQTRAIKEQLHKYVRELEQANDD----LERAKRATIVSLEDFEQRLNQAIERNAFLES 155
Cdd:COG5185   367 VG--EVELSKSSEE---LDSFKDTIESTKESLDEIPQNQRGYAQEilatLEDTLKAADRQIEELQRQIEQATSSNEEVSK 441
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1720368068 156 ELDEKESLLVSVQRLKDEARDLRQELAVRERQQEV 190
Cdd:COG5185   442 LLNELISELNKVMREADEESQSRLEEAYDEINRSV 476
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
12-190 3.63e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  12 LKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQlvqaeQRNRDLQADNQRLKYEVEALKEKLEH------ 85
Cdd:PRK02224  549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-----ERIRTLLAAIADAEDEIERLREKREAlaelnd 623
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  86 ----QYAQSYKQVSVLEDD-----LSQTRAIKEQLHKYVRELEQANDDLERAK---RATIVSLEDFEQRLNQAIERNAFL 153
Cdd:PRK02224  624 erreRLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERddlQAEIGAVENELEELEELRERREAL 703
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1720368068 154 ESELDEKESLLVSVQRLKDEARDLRQELavreRQQEV 190
Cdd:PRK02224  704 ENRVEALEALYDEAEELESMYGDLRAEL----RQRNV 736
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
32-180 4.64e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  32 EARDELV---EFQEGSRE----LEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQSYKQVSVLEDDL 101
Cdd:PRK02224  293 EERDDLLaeaGLDDADAEaveaRREELEDRDEELRDRLEECRVAAQAHNEEAESLREDaddLEERAEELREEAAELESEL 372
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720368068 102 SQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQE 180
Cdd:PRK02224  373 EEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEA 451
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
31-148 4.76e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 42.12  E-value: 4.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLqadnQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQT--RAIK 108
Cdd:PRK00409  505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEA----EALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqQAIK 580
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720368068 109 E------QLHKYVRELEQANDDLERAKRativsLEDFEQRLNQAIE 148
Cdd:PRK00409  581 EakkeadEIIKELRQLQKGGYASVKAHE-----LIEARKRLNKANE 621
PRK12705 PRK12705
hypothetical protein; Provisional
25-189 4.77e-04

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 42.00  E-value: 4.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  25 KYKQSFQEARDELVEFQEGSREL--EAELEAQLVQAEQRNRDLQADNQRlkyevealKEKLEHQYAQSYKQvsvleddls 102
Cdd:PRK12705   27 KRQRLAKEAERILQEAQKEAEEKleAALLEAKELLLRERNQQRQEARRE--------REELQREEERLVQK--------- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 103 qtraiKEQLHKYVRELEQANDDLERAKRAtivsledFEQRLNQAIERNAFLESELDEKESLLVSVQR---LKDEARDLRQ 179
Cdd:PRK12705   90 -----EEQLDARAEKLDNLENQLEEREKA-------LSARELELEELEKQLDNELYRVAGLTPEQARkllLKLLDAELEE 157
                         170
                  ....*....|
gi 1720368068 180 ELAVRERQQE 189
Cdd:PRK12705  158 EKAQRVKKIE 167
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
41-196 4.91e-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: 42.25  E-value: 4.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   41 QEGSRELEAELEAQLVQAEQRNRDLQadnQRLkyeveALKEKLEHQYAQSYKQVSVLEDDLSQTRA---IKEQLHKY--- 114
Cdd:COG3096    436 PENAEDYLAAFRAKEQQATEEVLELE---QKL-----SVADAARRQFEKAYELVCKIAGEVERSQAwqtARELLRRYrsq 507
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  115 -------------VRELEQANDDLERAKRativSLEDFEQRLNQAIERNAFLESELDE----KESLLVSVQRLKDEARDL 177
Cdd:COG3096    508 qalaqrlqqlraqLAELEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAEleaqLEELEEQAAEAVEQRSEL 583
                          170       180
                   ....*....|....*....|
gi 1720368068  178 RQEL-AVRERQQEVTRKsAP 196
Cdd:COG3096    584 RQQLeQLRARIKELAAR-AP 602
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
49-190 5.33e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 41.19  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  49 AELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKlehqyaqsykqvsvleddlsqtRAIKEQLHKYVRELEQANDDLERA 128
Cdd:COG1566    79 TDLQAALAQAEAQLAAAEAQLARLEAELGAEAEI----------------------AAAEAQLAAAQAQLDLAQRELERY 136
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720368068 129 KRAT---IVSLEDFEQRLNQAIErnafLESELDEKESLLVSVQRLKDEARDLRQ-ELAVRERQQEV 190
Cdd:COG1566   137 QALYkkgAVSQQELDEARAALDA----AQAQLEAAQAQLAQAQAGLREEEELAAaQAQVAQAEAAL 198
PRK13922 PRK13922
rod shape-determining protein MreC; Provisional
143-189 6.59e-04

rod shape-determining protein MreC; Provisional


Pssm-ID: 237560  Cd Length: 276  Bit Score: 40.73  E-value: 6.59e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1720368068 143 LNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQE 189
Cdd:PRK13922   71 LFDLREENEELKKELLELESRLQELEQLEAENARLRELLNLKESLDY 117
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
49-196 6.98e-04

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: 39.94  E-value: 6.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  49 AELEAQLVQAEQR-----NRDLQADNQRLKYEVEALKEKLEhQYAQSYKQvsVLEDDLSQTRAikeQLHKYVREL-EQAN 122
Cdd:pfam01442  14 EELQEQLGPVAQElvdrlEKETEALRERLQKDLEEVRAKLE-PYLEELQA--KLGQNVEELRQ---RLEPYTEELrKRLN 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720368068 123 DDLERAKRATIVSLEDFEQRLNQAIER-NAFLESELDE-KESLLVSVQRLKDEARDLRQEL--AVRERQQEVTRKSAP 196
Cdd:pfam01442  88 ADAEELQEKLAPYGEELRERLEQNVDAlRARLAPYAEElRQKLAERLEELKESLAPYAEEVqaQLSQRLQELREKLEP 165
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
32-195 7.96e-04

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: 41.50  E-value: 7.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   32 EARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQL 111
Cdd:pfam02463  153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  112 hKYVRELEQANDDLERAKRATIVSledfEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVT 191
Cdd:pfam02463  233 -KLNEERIDLLQELLRDEQEEIES----SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307

                   ....
gi 1720368068  192 RKSA 195
Cdd:pfam02463  308 RKVD 311
FtsB COG2919
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
49-84 8.21e-04

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


Pssm-ID: 442163 [Multi-domain]  Cd Length: 96  Bit Score: 38.32  E-value: 8.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1720368068  49 AELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLE 84
Cdd:COG2919    32 RELRQEIAELEAENAKLKARNAELEAEVADLKDGPD 67
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
10-181 9.71e-04

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: 40.88  E-value: 9.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  10 SSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEaqlvQAEQRNRDLQADNQRLKYEVEALKEkLEHQYAQ 89
Cdd:pfam05557 107 SCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKAS----EAEQLRQNLEKQQSSLAEAEQRIKE-LEFEIQS 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  90 SykqvsvlEDDLSQTRAIKEQLHKYvreleqanDDLERAKRAtivsLEDFEQRLNQAIERNAFLESELDEKESLLVSVQR 169
Cdd:pfam05557 182 Q-------EQDSEIVKNSKSELARI--------PELEKELER----LREHNKHLNENIENKLLLKEEVEDLKRKLEREEK 242
                         170
                  ....*....|..
gi 1720368068 170 LKDEARDLRQEL 181
Cdd:pfam05557 243 YREEAATLELEK 254
LRRFIP pfam09738
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ...
29-154 1.03e-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: 40.45  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  29 SFQEARDELVEFQEGSREleaeleAQLVQAeqrnrdlQADNQR--LKYEVEALKEKLEHqyaqsykqvsvLEDDLSQTRa 106
Cdd:pfam09738  87 SLRDIKHELKEVEEKYRK------AMISNA-------QLDNEKsnLMYQVDLLKDKLEE-----------MEESLAELQ- 141
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1720368068 107 ikeqlhkyvRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLE 154
Cdd:pfam09738 142 ---------RELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIE 180
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
44-200 1.13e-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: 40.48  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  44 SRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYkqvsvleddlSQTRAIKEQLHKYVRELEQAND 123
Cdd:pfam00529  56 YQAALDSAEAQLAKAQAQVARLQAELDRLQ-ALESELAISRQDYDGAT----------AQLRAAQAAVKAAQAQLAQAQI 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 124 DLERAK-RATI--VSLEDF-EQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELA-----VRERQQEVTRKS 194
Cdd:pfam00529 125 DLARRRvLAPIggISRESLvTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSgaqlqIAEAEAELKLAK 204

                  ....*.
gi 1720368068 195 APSSPT 200
Cdd:pfam00529 205 LDLERT 210
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
10-189 1.18e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.59  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  10 SSLKEETAYWKELSLK----YKQSFQEARDELVEFQEGSRELEAE--------LEAQLVQAEQRNRDLQADNQRLK---- 73
Cdd:PRK04778  201 DQLEEELAALEQIMEEipelLKELQTELPDQLQELKAGYRELVEEgyhldhldIEKEIQDLKEQIDENLALLEELDldea 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  74 -YEVEALKEKLEHQYAQ------SYKQV----SVLEDDLSQTRAIKEQLHKYVRELEQ----ANDDLERAKrativsleD 138
Cdd:PRK04778  281 eEKNEEIQERIDQLYDIlerevkARKYVeknsDTLPDFLEHAKEQNKELKEEIDRVKQsytlNESELESVR--------Q 352
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720368068 139 FEQRLNQAIERNAFLESELDEKESLLVSVQrlkDEARDLRQELAVRERQQE 189
Cdd:PRK04778  353 LEKQLESLEKQYDEITERIAEQEIAYSELQ---EELEEILKQLEEIEKEQE 400
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
9-194 1.18e-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: 40.71  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   9 FSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQlvqAEQRNRDLQADNQRLKyEVEALKEKLEHQYA 88
Cdd:COG5185   217 SESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQN---TDLRLEKLGENAESSK-RLNENANNLIKQFE 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  89 QSYKQVSVLEDDLSQTRAIkEQLHKYVRELEqANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQ 168
Cdd:COG5185   293 NTKEKIAEYTKSIDIKKAT-ESLEEQLAAAE-AEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEV 370
                         170       180
                  ....*....|....*....|....*.
gi 1720368068 169 RLKDEARDLRQElavrERQQEVTRKS 194
Cdd:COG5185   371 ELSKSSEELDSF----KDTIESTKES 392
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
14-189 1.30e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  14 EETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVealkekLEHQYAQSYKQ 93
Cdd:COG4717   305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE------LEQEIAALLAE 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  94 VSV-LEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDF-EQRLNQAIERNAFLESELDEK-ESLLVSVQRL 170
Cdd:COG4717   379 AGVeDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdEEELEEELEELEEELEELEEElEELREELAEL 458
                         170
                  ....*....|....*....
gi 1720368068 171 KDEARDLRQELAVRERQQE 189
Cdd:COG4717   459 EAELEQLEEDGELAELLQE 477
mukB PRK04863
chromosome partition protein MukB;
6-184 1.30e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.71  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068    6 IPDFSSLKEETaywkelslkYKQSFQEARDELVEFQEGSR----------ELEAEL------EAQLVQAEQRNRDLQADN 69
Cdd:PRK04863   881 LPRLNLLADET---------LADRVEEIREQLDEAEEAKRfvqqhgnalaQLEPIVsvlqsdPEQFEQLKQDYQQAQQTQ 951
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   70 QRLKYEVEALKEKLEHQYAQSYKQVsvlEDDLSQTRAIKEQLHkyvRELEQANDDLERAKRAtivsLEDFEQRLNQAIER 149
Cdd:PRK04863   952 RDAKQQAFALTEVVQRRAHFSYEDA---AEMLAKNSDLNEKLR---QRLEQAEQERTRAREQ----LRQAQAQLAQYNQV 1021
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1720368068  150 NAFLESELDEKEsllvsvQRLKDEARDLrQELAVR 184
Cdd:PRK04863  1022 LASLKSSYDAKR------QMLQELKQEL-QDLGVP 1049
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
54-193 1.36e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.39  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  54 QLVQAEQRNRDLQADNQRLKYEVEALK--------EKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDL 125
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNnqkeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNS 354
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720368068 126 ErakrativslEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELavreRQQEVTRK 193
Cdd:TIGR04523 355 E----------SENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKI----QNQEKLNQ 408
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
27-149 1.37e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.52  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  27 KQSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQ-----ADNQRlkyEVEALKEKLEHQyaqsYKQVSVLE 98
Cdd:COG1579    37 EDELAALEARLEAAKTELEDLEKEikrLELEIEEVEARIKKYEeqlgnVRNNK---EYEALQKEIESL----KRRISDLE 109
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720368068  99 DDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIER 149
Cdd:COG1579   110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
31-193 1.59e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   31 QEARDELVEFQEGSRELEAELEA--QLVQAEQRNRDLQADNQRLKYEVEALK--------EKLEHQYAQSYKQVSVLEDD 100
Cdd:COG4913    231 VEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRlwfaqrrlELLEAELEELRAELARLEAE 310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  101 LSQTRAIKEQLHKYVRELEQAN--------DDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQR--- 169
Cdd:COG4913    311 LERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAeaa 390
                          170       180
                   ....*....|....*....|....*
gi 1720368068  170 -LKDEARDLRQELAVRERQQEVTRK 193
Cdd:COG4913    391 aLLEALEEELEALEEALAEAEAALR 415
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
21-251 2.21e-03

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 39.73  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  21 ELSLKYKQsFQEARDEL-VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQ---------- 89
Cdd:pfam07111 478 DLSLELEQ-LREERNRLdAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQlevarqgqqe 556
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  90 SYKQVSVLEDDLSQTRAIKEQ-LHKYVRELE-----QANDDLERAKRA------TIVSLEDFEQRLNQAIERNAFLesel 157
Cdd:pfam07111 557 STEEAASLRQELTQQQEIYGQaLQEKVAEVEtrlreQLSDTKRRLNEArreqakAVVSLRQIQHRATQEKERNQEL---- 632
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 158 dekesllvsvQRLKDEARDLRQELAVReRQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENSFPSPKAIPN 237
Cdd:pfam07111 633 ----------RRLQDEARKEEGQRLAR-RVQELERDKNLMLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECS 701
                         250
                  ....*....|....
gi 1720368068 238 GFGTSPLTPSARIS 251
Cdd:pfam07111 702 ASAPIPAAVPTRES 715
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
41-195 2.25e-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: 39.88  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  41 QEGSRELEAELEAQLVQAEQRNRDlqadnqrlKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQ 120
Cdd:pfam07888  37 EECLQERAELLQAQEAANRQREKE--------KERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720368068 121 ANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLvsvQRLKDeardlRQELAVRERQQEVTRKSA 195
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETEL---ERMKE-----RAKKAGAQRKEEEAERKQ 175
PRK12704 PRK12704
phosphodiesterase; Provisional
13-173 2.48e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  13 KEEtayWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKY---EVEALKEKLEHQYAq 89
Cdd:PRK12704   63 KEE---IHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQkqqELEKKEEELEELIE- 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  90 syKQVSVLED--DLSQTRAiKEQLhkyvreLEQANDDLERAKRATIvsledfeqrlnQAIERNAFLESELDEKESLLVSV 167
Cdd:PRK12704  139 --EQLQELERisGLTAEEA-KEIL------LEKVEEEARHEAAVLI-----------KEIEEEAKEEADKKAKEILAQAI 198

                  ....*.
gi 1720368068 168 QRLKDE 173
Cdd:PRK12704  199 QRCAAD 204
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
20-189 2.90e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 2.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  20 KELSLKYKQSFQEARDELVEFQEGSRELEaELEAQLVQAEQRNRDLQADNQRLKYE-VEALKEKLEhQYAQSYKQVSVLE 98
Cdd:PRK03918  531 KEKLIKLKGEIKSLKKELEKLEELKKKLA-ELEKKLDELEEELAELLKELEELGFEsVEELEERLK-ELEPFYNEYLELK 608
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  99 DDLSQTRAIKEQLHKYVRELEQANDDLERAKRA------------TIVSLEDFEQRLNQAIERNAFLESELDEKESLLVS 166
Cdd:PRK03918  609 DAEKELEREEKELKKLEEELDKAFEELAETEKRleelrkeleeleKKYSEEEYEELREEYLELSRELAGLRAELEELEKR 688
                         170       180
                  ....*....|....*....|...
gi 1720368068 167 VQRLKDEARDLRQELAVRERQQE 189
Cdd:PRK03918  689 REEIKKTLEKLKEELEEREKAKK 711
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
28-193 3.00e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.39  E-value: 3.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   28 QSFQEARDELVEFQEgsrELEAElEAQLVQAEQRNRDLQAdnqrlkyEVEALKEKLEhqyaqsykqvsvleDDLSQTRAI 107
Cdd:pfam01576  264 KKIRELEAQISELQE---DLESE-RAARNKAEKQRRDLGE-------ELEALKTELE--------------DTLDTTAAQ 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  108 KEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIER-NAFLESELDEKESLLVSVQRLKDEARDLRQEL-AVRE 185
Cdd:pfam01576  319 QELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEElTEQLEQAKRNKANLEKAKQALESENAELQAELrTLQQ 398

                   ....*...
gi 1720368068  186 RQQEVTRK 193
Cdd:pfam01576  399 AKQDSEHK 406
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
27-179 3.62e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  27 KQSFQEARDELVEFQEGSRELEAELEA----------QLVQAEQRNRDLQADNQRLKYEVEAL---KEKLEHQYAQSYKQ 93
Cdd:COG4372    65 EEELEQARSELEQLEEELEELNEQLQAaqaelaqaqeELESLQEEAEELQEELEELQKERQDLeqqRKQLEAQIAELQSE 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  94 VSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVsledfeQRLNQAIERNAFLESELDEKESLLVSVQRLKDE 173
Cdd:COG4372   145 IAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL------DELLKEANRNAEKEEELAEAEKLIESLPRELAE 218

                  ....*.
gi 1720368068 174 ARDLRQ 179
Cdd:COG4372   219 ELLEAK 224
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
8-129 3.85e-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: 39.28  E-value: 3.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068    8 DFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELE---AELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLE 84
Cdd:TIGR02169  379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSeelADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1720368068   85 HQYAQsykqvsvLEDDLSQTRAIKEQLHKYVRELEQANDDLERAK 129
Cdd:TIGR02169  459 QLAAD-------LSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
41-177 3.87e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  41 QEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHkyvRELEQ 120
Cdd:COG1196   670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL---LEEEE 746
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 121 ANDDLERAKRATIVSLEDFEQRLNQ--------------AIE-------RNAFLESELD----EKESLLVSVQRLKDEAR 175
Cdd:COG1196   747 LLEEEALEELPEPPDLEELERELERlereiealgpvnllAIEeyeeleeRYDFLSEQREdleeARETLEEAIEEIDRETR 826

                  ..
gi 1720368068 176 DL 177
Cdd:COG1196   827 ER 828
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
32-194 3.92e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.00  E-value: 3.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   32 EARDELVEFQEGSRELEAELEAQlVQAEQRNRDLQADNQRL----------KYEVEALKEKLEHQYAQSYKQVSVLEDDL 101
Cdd:pfam01576  630 EAREKETRALSLARALEEALEAK-EELERTNKQLRAEMEDLvsskddvgknVHELERSKRALEQQVEEMKTQLEELEDEL 708
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  102 SQTRAIKEQLH--------KYVRELeQANDDLERAKRATIVS--------LEDFEQRLNQAIERNAFLESELDEKESLLV 165
Cdd:pfam01576  709 QATEDAKLRLEvnmqalkaQFERDL-QARDEQGEEKRRQLVKqvreleaeLEDERKQRAQAVAAKKKLELDLKELEAQID 787
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1720368068  166 SVQRLKDEA----RDLRQELAVRERQQEVTRKS 194
Cdd:pfam01576  788 AANKGREEAvkqlKKLQAQMKDLQRELEEARAS 820
PilN COG3166
Type IV pilus assembly protein PilN [Cell motility, Extracellular structures];
139-189 3.99e-03

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


Pssm-ID: 442399 [Multi-domain]  Cd Length: 185  Bit Score: 37.64  E-value: 3.99e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720368068 139 FEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQE 189
Cdd:COG3166    43 LQGQIAQQQARNAALQQEIAKLDKQIAEIKELKKQKAELLARLQVIEQLQQ 93
PRK12704 PRK12704
phosphodiesterase; Provisional
34-189 4.02e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  34 RDELVEFQEGSRELEAELEAQLvqaEQRNRDLQADNQRLKYEVEALKEKLEhqyaqsykQVSVLEDDLSQTRAIKEQLHK 113
Cdd:PRK12704   56 KEALLEAKEEIHKLRNEFEKEL---RERRNELQKLEKRLLQKEENLDRKLE--------LLEKREEELEKKEKELEQKQQ 124
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720368068 114 YVRELEQanddlerakrativSLEDFEQRLNQAIERNAFLESElDEKESLLvsvQRLKDEArdlRQELAVRERQQE 189
Cdd:PRK12704  125 ELEKKEE--------------ELEELIEEQLQELERISGLTAE-EAKEILL---EKVEEEA---RHEAAVLIKEIE 179
mukB PRK04863
chromosome partition protein MukB;
28-179 4.34e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 4.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   28 QSFQEARDELVEFqEGSRELEAELEAQLVQAEQR-NRDLQ--ADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQT 104
Cdd:PRK04863   513 EQLQQLRMRLSEL-EQRLRQQQRAERLLAEFCKRlGKNLDdeDELEQLQEELEARLESLSESVSEARERRMALRQQLEQL 591
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720368068  105 RAIKEQLHKYVRELEQANDDLERAKRATIVSLEDfEQRLNQAIERNAFLESELDEKESLLVS-VQRLKDEARDLRQ 179
Cdd:PRK04863   592 QARIQRLAARAPAWLAAQDALARLREQSGEEFED-SQDVTEYMQQLLERERELTVERDELAArKQALDEEIERLSQ 666
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
49-194 4.69e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.84  E-value: 4.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  49 AELEAQLVQAEQRNRDLQADNQRLKYEVEALkeklehqyaQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERA 128
Cdd:COG3206   185 PELRKELEEAEAALEEFRQKNGLVDLSEEAK---------LLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDA 255
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 129 KRATIVSledfeQRLNQAIERNAFLESELDEKESLLV----SVQRLKDEARDLRQELAVRERQQEVTRKS 194
Cdd:COG3206   256 LPELLQS-----PVIQQLRAQLAELEAELAELSARYTpnhpDVIALRAQIAALRAQLQQEAQRILASLEA 320
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
38-181 4.71e-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: 39.17  E-value: 4.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   38 VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEhQYAQSYKQVSVLEDDLSQTRaikeqlhkyVRE 117
Cdd:COG3096    828 VAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQ-LLNKLLPQANLLADETLADR---------LEE 897
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720368068  118 LEQANDDLERAKRativSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQEL 181
Cdd:COG3096    898 LREELDAAQEAQA----FIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQI 957
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
13-193 4.76e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 4.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  13 KEETAYwkELSLKYKQSFQEARDELVEFQEGSRELE---AELEAQLVQAEQRNRDLQADNQRLKYEVEALK--------- 80
Cdd:PRK03918  159 DYENAY--KNLGEVIKEIKRRIERLEKFIKRTENIEeliKEKEKELEEVLREINEISSELPELREELEKLEkevkeleel 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  81 ----EKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLE--RAKRATIVSLEDFEQRLNQAIERnafLE 154
Cdd:PRK03918  237 keeiEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELRE---IE 313
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720368068 155 SELDEKESLLVSVQRLKDEARDLRQELA-VRERQQEVTRK 193
Cdd:PRK03918  314 KRLSRLEEEINGIEERIKELEEKEERLEeLKKKLKELEKR 353
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
28-192 5.00e-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: 38.78  E-value: 5.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   28 QSFQEARDELVEF--QEGSRELEAELEAQLVQAEQRNRDLQadnqrlkyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTR 105
Cdd:COG3096    492 QAWQTARELLRRYrsQQALAQRLQQLRAQLAELEQRLRQQQ--------NAERLLEEFCQRIGQQLDAAEELEELLAELE 563
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  106 AIKEQLHKYVRELEQANDDLER---AKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQrlkdearDLRQELA 182
Cdd:COG3096    564 AQLEELEEQAAEAVEQRSELRQqleQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVT-------AAMQQLL 636
                          170
                   ....*....|
gi 1720368068  183 VRERQQEVTR 192
Cdd:COG3096    637 EREREATVER 646
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
11-188 5.06e-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: 38.80  E-value: 5.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   11 SLKEETAYWKElSLKYK--------QSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQrlkyevEALKEk 82
Cdd:TIGR00618  687 SEKEQLTYWKE-MLAQCqtllreleTHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR------TVLKA- 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   83 LEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLN----QAIERNAFLESELD 158
Cdd:TIGR00618  759 RTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlqceTLVQEEEQFLSRLE 838
                          170       180       190
                   ....*....|....*....|....*....|
gi 1720368068  159 EKESLLVSVQRLKDEARDLRQELAVRERQQ 188
Cdd:TIGR00618  839 EKSATLGEITHQLLKYEECSKQLAQLTQEQ 868
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
35-182 5.44e-03

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: 38.67  E-value: 5.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   35 DELVEFQEGSRELEAELEAQLVQAEQRNRD-LQADNQRLKYEVEALKEKLEHQYAQsYKQVSVLEDDLSQTRAIKEQLHK 113
Cdd:pfam12128  397 DKLAKIREARDRQLAVAEDDLQALESELREqLEAGKLEFNEEEYRLKSRLGELKLR-LNQATATPELLLQLENFDERIER 475
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720368068  114 YVRELEQANDDLERAKRATIVSLEDFEQ---RLNQAIERNAFLESELDEKESLLVS-----VQRLKDEARDLRQELA 182
Cdd:pfam12128  476 AREEQEAANAEVERLQSELRQARKRRDQaseALRQASRRLEERQSALDELELQLFPqagtlLHFLRKEAPDWEQSIG 552
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
33-194 5.49e-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: 38.90  E-value: 5.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   33 ARDELVEFQEGSRELEaELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEhqyaQSYKQVSVLEDDLSQTRAIKEQLH 112
Cdd:TIGR02169  669 SRSEPAELQRLRERLE-GLKRELSSLQSELRRIENRLDELSQELSDASRKIG----EIEKEIEQLEQEEEKLKERLEELE 743
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  113 KYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKEsllvsVQRLKDEARDL-----RQELAVRERQ 187
Cdd:TIGR02169  744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR-----IPEIQAELSKLeeevsRIEARLREIE 818

                   ....*..
gi 1720368068  188 QEVTRKS 194
Cdd:TIGR02169  819 QKLNRLT 825
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
12-127 5.51e-03

Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).


Pssm-ID: 464620 [Multi-domain]  Cd Length: 276  Bit Score: 38.15  E-value: 5.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  12 LKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAqlVQAEQRNRDLQADN----QRLKYEVEALKEKLEHQY 87
Cdd:pfam15294 131 LHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKD--LQKEQGAKKDVKSNlkeiSDLEEKMAALKSDLEKTL 208
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1720368068  88 AQSYKQVSVLEDDLSQTraiKEQLHKYVRELEQANDDLER 127
Cdd:pfam15294 209 NASTALQKSLEEDLAST---KHELLKVQEQLEMAEKELEK 245
PRKG1_interact pfam15898
cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of ...
98-177 6.61e-03

cGMP-dependent protein kinase interacting domain; This domain is found at the C-terminus of protein phosphatase 1 regulatory subunits 12A, 12B and 12C. In protein phosphatase 1 regulatory subunit 12A it has been found to bind to cGMP-dependent protein kinase 1 via a leucine zipper motif located at the C-terminus of this domain.


Pssm-ID: 464927 [Multi-domain]  Cd Length: 102  Bit Score: 35.74  E-value: 6.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  98 EDDLSQTRAIKEQLHKYVRELEQANDDLERA---------KRATIVSLEDFEQRlnqAIERNAF-LESELDEKESLLVSV 167
Cdd:pfam15898   7 EEELQENERLKRKLQDAQQELAELKSQLERLtqqrqesfsDRSSLLETEKREKR---ALERKISeMEEELKVLEDLRAEN 83
                          90
                  ....*....|
gi 1720368068 168 QRLKDEARDL 177
Cdd:pfam15898  84 QRLKDENGAL 93
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
26-192 7.22e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.48  E-value: 7.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  26 YKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRnrDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLeDDLSQTR 105
Cdd:PRK02224  167 YRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETR-DEADEVL 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 106 AIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLvSVQRLKDEARDLRQElAVRE 185
Cdd:PRK02224  244 EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA-GLDDADAEAVEARRE-ELED 321

                  ....*..
gi 1720368068 186 RQQEVTR 192
Cdd:PRK02224  322 RDEELRD 328
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
32-199 7.29e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 7.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  32 EARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEhqyaqsykqvsVLEDDLSQTRAIKEQL 111
Cdd:PRK03918  224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE-----------ELEEKVKELKELKEKA 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 112 HKYvRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLES------ELDEKES-LLVSVQRLKDEARDLRQELAVR 184
Cdd:PRK03918  293 EEY-IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeerleELKKKLKeLEKRLEELEERHELYEEAKAKK 371
                         170
                  ....*....|....*
gi 1720368068 185 ERQQEVTRKSAPSSP 199
Cdd:PRK03918  372 EELERLKKRLTGLTP 386
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
65-206 7.39e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 7.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   65 LQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHK-------------YVRELEQANDDLERAkRA 131
Cdd:COG4913    604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvasAEREIAELEAELERL-DA 682
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720368068  132 TIVSLEDFEQRLNQAIERNAFLESELDEkesLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSPTLDCEKM 206
Cdd:COG4913    683 SSDDLAALEEQLEELEAELEELEEELDE---LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEER 754
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
4-179 8.27e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.21  E-value: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   4 EDIPDFSSLKEETAYWKELSLKYK-QSFQEARDELveFQEGSRELEAELEAQLVQAEQRN---RDLQADNQRLKYEVEAL 79
Cdd:COG4717   341 ELLDRIEELQELLREAEELEEELQlEELEQEIAAL--LAEAGVEDEEELRAALEQAEEYQelkEELEELEEQLEELLGEL 418
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  80 KEKLE-HQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRativsLEDFEQRLNQAIERNAFLESELD 158
Cdd:COG4717   419 EELLEaLDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAELRELAEEWA 493
                         170       180
                  ....*....|....*....|.
gi 1720368068 159 EKESLLVSVQRLKDEARDLRQ 179
Cdd:COG4717   494 ALKLALELLEEAREEYREERL 514
PRK14146 PRK14146
heat shock protein GrpE; Provisional
28-127 8.48e-03

heat shock protein GrpE; Provisional


Pssm-ID: 172635 [Multi-domain]  Cd Length: 215  Bit Score: 37.02  E-value: 8.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  28 QSFQEARDELVEFQEGSRELEaELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYA--QSYKQVSVleDDLSQTR 105
Cdd:PRK14146   23 QTLEESKLENMNSEESQTITE-ETQEQAVEGAETETSLQKELDNAKKEIESLKDSWARERAefQNFKRRSA--QEFVSIR 99
                          90       100
                  ....*....|....*....|..
gi 1720368068 106 aiKEQLHKYVRELEQANDDLER 127
Cdd:PRK14146  100 --KEAVKSLVSGFLNPIDNLER 119
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
31-189 8.65e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 38.23  E-value: 8.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068   31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKqvsvLEDDLSQTRAIKEQ 110
Cdd:pfam01576   60 EEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQK----LQLEKVTTEAKIKK 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  111 LHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQ-RLKDEARdLRQELAVRERQQE 189
Cdd:pfam01576  136 LEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEeRLKKEEK-GRQELEKAKRKLE 214
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
36-185 9.24e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 37.04  E-value: 9.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068  36 ELVEFQEGSRELEAELEA--QLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQyAQSYKQVSVLEDDLSQTRAI-KEQLH 112
Cdd:cd00176     1 KLQQFLRDADELEAWLSEkeELLSSTDYGDDLESVEALLK-KHEALEAELAAH-EERVEALNELGEQLIEEGHPdAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720368068 113 KYVRELEQANDDLERAkrativsLEDFEQRLNQAIERNAF------LESELDEKESLLVS---------VQRLKDEARDL 177
Cdd:cd00176    79 ERLEELNQRWEELREL-------AEERRQRLEEALDLQQFfrdaddLEQWLEEKEAALASedlgkdlesVEELLKKHKEL 151

                  ....*...
gi 1720368068 178 RQELAVRE 185
Cdd:cd00176   152 EEELEAHE 159
 
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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