|
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 238550188 135 SLEDFEQRLNQAIERNAFLESEL----DEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSP---TLDCEKMD 207
Cdd:pfam04880 1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKLRNLLMRSPSTPslqTLEIFDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 208 SAVQASlslpATPVG-KGTENSFPSpkAIPNGFGTSPLTPSARISAlnivgDLLRKVGALESKLAACRNFAKDQASRKSY 286
Cdd:pfam04880 81 PAVQAV----SSPVIaTPPEKSFNS--LRTGSETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNASRRG 149
|
170 180
....*....|....*....|...
gi 238550188 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 238550188 27 KQSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAqsykQVSVLEDDLSQ 103
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEEELAELEEELEELEE----ELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 104 TRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAV 183
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
170
....*....|..
gi 238550188 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 238550188 24 LKYKQSFQEARDELVEFQEGSRELEAELEA---QLVQAEQRNRDLQADNQRLKYEVEALKEklehQYAQSYKQVSVLEDD 100
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAElrkELEELEEELEQLRKELEELSRQISALRK----DLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 101 LSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESllvSVQRLKDEARDLRQE 180
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANLRER 825
|
170
....*....|....*
gi 238550188 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 238550188 27 KQSFQEARDELVEFQEGSRELEaELEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQS-YKQVSVLEDDLS 102
Cdd:COG4913 270 RLAELEYLRAALRLWFAQRRLE-LLEAELEELRAELARLEAELERLEARLDALREEldeLEAQIRGNgGDRLEQLEREIE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 103 QTRAIKEQLhkyVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKE----SLLVSVQRLKDEARDLR 178
Cdd:COG4913 349 RLERELEER---ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEealaEAEAALRDLRRELRELE 425
|
170
....*....|
gi 238550188 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 238550188 13 KEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQ 89
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyeLLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 90 SYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQR 169
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180
....*....|....*....|....*...
gi 238550188 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 238550188 27 KQSFQEARDELVEFQEGSRELEaELEAQLVQAEQRNRDLQADNQRLKYEVEAL-----KEKLEHQYAQSYKQVSVLEDDL 101
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLLQLLplyqeLEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 102 SQTRAIKEQLHKYVRELEQANDDLERAKRATivsLEDFEQRLNQAIERNAFLESELDEKESLLvsvQRLKDEARDLRQEL 181
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQL---SLATEEELQDLAEELEELQQRLAELEEEL---EEAQEELEELEEEL 229
|
170
....*....|..
gi 238550188 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 238550188 27 KQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRA 106
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 107 IKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLvsvQRLKDEARDLRQELAVRER 186
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI---EELESELEALLNERASLEE 887
|
....*..
gi 238550188 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 238550188 45 RELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHqyAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDD 124
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREA--LQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 125 LERAKR---ATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDL------------RQELAVRERQQE 189
Cdd:COG4913 687 LAALEEqleELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelralleerFAAALGDAVERE 766
|
...
gi 238550188 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 238550188 31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYaQSYKQVSVLE------------ 98
Cdd:COG3883 40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY-RSGGSVSYLDvllgsesfsdfl 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 99 DDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLR 178
Cdd:COG3883 119 DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 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 238550188 31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQ 110
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA-EAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238550188 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 238550188 10 SSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEA---ELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQ 86
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 87 YAQSYK--QVSVLE-----DDLSQT-------RAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAF 152
Cdd:COG4942 110 LRALYRlgRQPPLAlllspEDFLDAvrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238550188 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 238550188 8 DFSSLKEETAYWkELSLKYKqsfqEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQY 87
Cdd:TIGR02169 215 ALLKEKREYEGY-ELLKEKE----ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 88 AQSYKQVSVLEDDLSQTRAIKEQLHKYVRELE--QANDDLERakRATIVSLEDFEQRLNQAIERNAFLESELDEK----E 161
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLERSIAEKERELEDAEerLAKLEAEI--DKLLAEIEELEREIEEERKRRDKLTEEYAELkeelE 367
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 238550188 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 238550188 20 KELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEhqyaQSYKQVSVLEd 99
Cdd:TIGR02168 227 LALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY----ALANEISRLE- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 100 dlSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDF---EQRLNQAIERNAFLESELDEKESLLV----SVQRLKD 172
Cdd:TIGR02168 302 --QQKQILRERLANLERQLEELEAQLEELESKLDELAEELaelEEKLEELKEELESLEAELEELEAELEelesRLEELEE 379
|
170 180
....*....|....*....|.
gi 238550188 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 238550188 31 QEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAI 107
Cdd:COG1196 305 ARLEERRRELEERLEELEEElaeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 108 KEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQ 187
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
....*...
gi 238550188 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 238550188 4 EDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQ---LVQAEQRNRDLQADNQRLKYEVEALK 80
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLrskVAQLELQIASLNNEIERLEARLERLE 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 81 --------EKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAF 152
Cdd:TIGR02168 414 drrerlqqEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
170 180
....*....|....*....|....*
gi 238550188 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 238550188 39 EFQEGSRELEAELeaQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVREL 118
Cdd:COG1196 217 ELKEELKELEAEL--LLLKLRELEAELEELEAELE-ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238550188 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 238550188 31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEq 110
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-DLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 111 LHKYVRELEQA---NDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKEsllvsvQRLKDEARDLRQELAVRERQ 187
Cdd:COG1579 91 YEALQKEIESLkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK------AELDEELAELEAELEELEAE 164
|
....*....
gi 238550188 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 238550188 20 KELSLKYKQSFQEARDELVEFQEGSRELEA----------------ELEAQLVQAEQRNRDLQADNQRLKY--------- 74
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEaeekeeeyaelqeeleELEEELEELEAELEELREELEKLEKllqllplyq 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 75 EVEALKEKLEH---QYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATivsLEDFEQRLNQAIERNA 151
Cdd:COG4717 133 ELEALEAELAElpeRLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE---LQDLAEELEELQQRLA 209
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 238550188 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 238550188 25 KYKQSFQEARDELVEFQEGSRELEAELEA---QLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDL 101
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 102 SQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDF---EQRLNQAIERNAFLESELDEKESllvSVQRLKDEARDLR 178
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERaslEEALALLRSELEELSEELRELES---KRSELRRELEELR 921
|
170
....*....|..
gi 238550188 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 238550188 10 SSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQ------ADNQRLKYEVEALKEKL 83
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSsleqeiENVKSELKELEARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 84 EHQYAQSYKQVSVLEDDLSQTRaikeqlhkyVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESL 163
Cdd:TIGR02169 771 EEDLHKLEEALNDLEARLSHSR---------IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
170 180 190
....*....|....*....|....*....|....
gi 238550188 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 238550188 12 LKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELE---AELEAQLVQAEQRNRDLQADNQRLKYEVEALK---EKLEH 85
Cdd:TIGR02168 794 LKEELKALREALDELRAELTLLNEEAANLRERLESLErriAATERRLEDLEEQIEELSEDIESLAAEIEELEeliEELES 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 86 QYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLV 165
Cdd:TIGR02168 874 ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL 953
|
170 180
....*....|....*....|....*....
gi 238550188 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 238550188 12 LKEETAYWKELSLKYKQSFQEARDELVEFqegsRELEAELEAQLVQAEQrnrdlQADNQRLKYevealkEKLEHQYAQSY 91
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEEL----EAELEELESRLEELEE-----QLETLRSKV------AQLELQIASLN 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 92 KQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVS-----LEDFEQRLNQAIERNAFLESELDEKESLLVS 166
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEeleeeLEELQEELERLEEALEELREELEEAEQALDA 479
|
170 180
....*....|....*....|...
gi 238550188 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 238550188 30 FQEARDELVEFQE---GSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQ---YAQSYKQVSVLEDDLSQ 103
Cdd:TIGR02168 276 VSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEELKEELES 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 104 TRAIKEQLHKYVRELEQANDDLERAkrativsLEDFEQRLNQAIERNAFLESELdekESLLVSVQRLKDEARDLRQELAV 183
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQ-------LETLRSKVAQLELQIASLNNEI---ERLEARLERLEDRRERLQQEIEE 425
|
170
....*....|..
gi 238550188 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 238550188 27 KQSFQEARDEL----VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKE-----KLEHQYA-QSYKQV-- 94
Cdd:pfam12128 645 RTALKNARLDLrrlfDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEeqkeqKREARTEkQAYWQVve 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 95 ---SVLEDDLSQTRAIKEQLHK---------YVREL------EQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESE 156
Cdd:pfam12128 725 galDAQLALLKAAIAARRSGAKaelkaletwYKRDLaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQET 804
|
170 180 190
....*....|....*....|....*....|....*..
gi 238550188 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 238550188 12 LKEETAYWKElslkYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALK----------E 81
Cdd:TIGR02169 838 LQEQRIDLKE----QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELErkieeleaqiE 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 82 KLEHQYAQSYKQVSVLEDDLSQTRAIK-------------EQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIE 148
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELSEIEDPKgedeeipeeelslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE 993
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238550188 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 238550188 24 LKYKQSFQEARDELVEFQEGSRELE---AELEAQLV----QAE--QRNRDLQADNQRLK-----YEVEALKEKLEH---Q 86
Cdd:TIGR02168 168 SKYKERRKETERKLERTRENLDRLEdilNELERQLKslerQAEkaERYKELKAELRELElallvLRLEELREELEElqeE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 87 YAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVS 166
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190
....*....|....*....|....*....|
gi 238550188 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 238550188 27 KQSFQEARDELVEFQEGSRELEAELEA-----QLVQAEQRnrdLQADNQRLKYEVEALKEKLEHQ---YAQSYKQVSVLE 98
Cdd:COG3096 305 QYRLVEMARELEELSARESDLEQDYQAasdhlNLVQTALR---QQEKIERYQEDLEELTERLEEQeevVEEAAEQLAEAE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 99 DDLSQTRA----IKEQLHKYVRELE----------QANDDLERAKR---ATIVSLEDFEQRLnqaiernafleSELDEKE 161
Cdd:COG3096 382 ARLEAAEEevdsLKSQLADYQQALDvqqtraiqyqQAVQALEKARAlcgLPDLTPENAEDYL-----------AAFRAKE 450
|
170 180
....*....|....*....|..
gi 238550188 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 238550188 22 LSLKyKQSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKekleHQYAQSYKQVSVLE 98
Cdd:PRK09039 69 LSLE-RQGNQDLQDSVANLRASLSAAEAErsrLQALLAELAGAGAAAEGRAGELAQELDSEK----QVSARALAQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 238550188 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 238550188 27 KQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRA 106
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE-QLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 107 IKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRER 186
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
....*..
gi 238550188 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 238550188 25 KYKQSFQEARDELVEFQE--GSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEH-------------- 85
Cdd:COG3206 186 ELRKELEEAEAALEEFRQknGLVDLSEEaklLLQQLSELESQLAEARAELAEAEARLAALRAQLGSgpdalpellqspvi 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 86 -QYAQSYKQVSVLEDDLSQT--------RAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERnafLESE 156
Cdd:COG3206 266 qQLRAQLAELEAELAELSARytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQ---LEAR 342
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 238550188 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 238550188 20 KELSLKYKQSFQEARDELVEFQEGSRELEAEL---------EAQLVQAEQRNRDLQADNQRLK-YEVEALK------EKL 83
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELrelekvlkkESELIKLKELAEQLKELEEKLKkYNLEELEkkaeeyEKL 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 84 EHQYAQSYKQVSVLEDDL-------SQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESE 156
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELekleelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDA 610
|
170 180 190
....*....|....*....|....*....|....*..
gi 238550188 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 238550188 12 LKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELE-----AELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQ 86
Cdd:TIGR00618 251 AQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaAPLAAHIKAVTQIEQQAQRIHTELQ-SKMRSRAKLLMK 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 87 YAQSYKQvsvlEDDLSQTRAIKEQLHKYVRELEQANDD----LERAKRATIVS--LEDFEQRLNQAIERNAFLESELDEK 160
Cdd:TIGR00618 330 RAAHVKQ----QSSIEEQRRLLQTLHSQEIHIRDAHEVatsiREISCQQHTLTqhIHTLQQQKTTLTQKLQSLCKELDIL 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 238550188 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 238550188 41 QEGSRELEAELEaQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRA----IKEQLHKYVR 116
Cdd:COG4942 19 ADAAAEAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAelaeLEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 117 ELEQANDDLERAKRAT-----------IVSLEDFEQ--RLNQAIER-NAFLESELDEKESLLVSVQRLKDEARDLRQELA 182
Cdd:COG4942 98 ELEAQKEELAELLRALyrlgrqpplalLLSPEDFLDavRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170
....*....|..
gi 238550188 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 238550188 31 QEARDELVEFQEGSRELEA------ELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQ--------SYKQVSV 96
Cdd:COG4913 671 AELEAELERLDASSDDLAAleeqleELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaedlaRLELRAL 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 97 LEDDLSQ----------TRAIKEQLHKYVRELEQANDDLERAKR--------------ATIVSLEDFEQRLNQAIE---- 148
Cdd:COG4913 751 LEERFAAalgdaverelRENLEERIDALRARLNRAEEELERAMRafnrewpaetadldADLESLPEYLALLDRLEEdglp 830
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 238550188 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 238550188 38 VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALK--EKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYV 115
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDriERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 116 RELE--------QANDDLERA--KRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLkdeaRDLRQELAVRE 185
Cdd:PRK02224 547 AELEaeaeekreAAAEAEEEAeeAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERL----REKREALAELN 622
|
..
gi 238550188 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 238550188 12 LKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSY 91
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 92 KQVSVLeddLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDfeqrLNQAIERNAFLESELdekESLLVSVQRLK 171
Cdd:pfam05483 240 KQVSLL---LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDEN----LKELIEKKDHLTKEL---EDIKMSLQRSM 309
|
170
....*....|..
gi 238550188 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 238550188 32 EARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQSYKQVSVLEDDLSQTR 105
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEvsrIEARLREIEQKLNRLTLEKEYLEKEIQELQEQridLKEQIKSIEKEIENLNGKKEELE 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 106 AIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQaiernafLESELDEKESLLvsvQRLKDEARDLRQELAVRE 185
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-------LEAQIEKKRKRL---SELKAKLEALEEELSEIE 937
|
170 180
....*....|....*....|....*..
gi 238550188 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 238550188 35 DELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQrlkyevealkeklehQYAQSYKQVSVLEDDLSQTRAIK------ 108
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHS---------------QFEQAYQLVRKIAGEVSRSEAWDvarell 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 109 -------------EQLHKYVRELEQANDDLERAKRAtivsLEDFEQRLNQAIERNAFLESELDEKESLLVSvqrLKDEAR 175
Cdd:PRK04863 503 rrlreqrhlaeqlQQLRMRLSELEQRLRQQQRAERL----LAEFCKRLGKNLDDEDELEQLQEELEARLES---LSESVS 575
|
170
....*....|....
gi 238550188 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 238550188 45 RELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQyaQSYKQvsvledDLSQTRAIKEQLHKYVRELEQANDD 124
Cdd:pfam13851 39 KKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENY--EKDKQ------SLKNLKARLKVLEKELKDLKWEHEV 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 238550188 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 238550188 6 IPDFSSLKEETA-YWKELSLK-----YKQSFQEARdELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEAL 79
Cdd:COG5185 288 IKQFENTKEKIAeYTKSIDIKkatesLEEQLAAAE-AEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENI 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 80 KEklEHQYAQSYKQvsvLEDDLSQTRAIKEQLHKYVRELEQANDD----LERAKRATIVSLEDFEQRLNQAIERNAFLES 155
Cdd:COG5185 367 VG--EVELSKSSEE---LDSFKDTIESTKESLDEIPQNQRGYAQEilatLEDTLKAADRQIEELQRQIEQATSSNEEVSK 441
|
170 180 190
....*....|....*....|....*....|....*
gi 238550188 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 238550188 12 LKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQlvqaeQRNRDLQADNQRLKYEVEALKEKLEH------ 85
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-----ERIRTLLAAIADAEDEIERLREKREAlaelnd 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 86 ----QYAQSYKQVSVLEDD-----LSQTRAIKEQLHKYVRELEQANDDLERAK---RATIVSLEDFEQRLNQAIERNAFL 153
Cdd:PRK02224 624 erreRLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERddlQAEIGAVENELEELEELRERREAL 703
|
170 180 190
....*....|....*....|....*....|....*..
gi 238550188 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 238550188 32 EARDELV---EFQEGSRE----LEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQSYKQVSVLEDDL 101
Cdd:PRK02224 293 EERDDLLaeaGLDDADAEaveaRREELEDRDEELRDRLEECRVAAQAHNEEAESLREDaddLEERAEELREEAAELESEL 372
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 238550188 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 238550188 31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLqadnQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQT--RAIK 108
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEA----EALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqQAIK 580
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 238550188 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 238550188 25 KYKQSFQEARDELVEFQEGSREL--EAELEAQLVQAEQRNRDLQADNQRlkyevealKEKLEHQYAQSYKQvsvleddls 102
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKleAALLEAKELLLRERNQQRQEARRE--------REELQREEERLVQK--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 103 qtraiKEQLHKYVRELEQANDDLERAKRAtivsledFEQRLNQAIERNAFLESELDEKESLLVSVQR---LKDEARDLRQ 179
Cdd:PRK12705 90 -----EEQLDARAEKLDNLENQLEEREKA-------LSARELELEELEKQLDNELYRVAGLTPEQARkllLKLLDAELEE 157
|
170
....*....|
gi 238550188 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 238550188 41 QEGSRELEAELEAQLVQAEQRNRDLQadnQRLkyeveALKEKLEHQYAQSYKQVSVLEDDLSQTRA---IKEQLHKY--- 114
Cdd:COG3096 436 PENAEDYLAAFRAKEQQATEEVLELE---QKL-----SVADAARRQFEKAYELVCKIAGEVERSQAwqtARELLRRYrsq 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 115 -------------VRELEQANDDLERAKRativSLEDFEQRLNQAIERNAFLESELDE----KESLLVSVQRLKDEARDL 177
Cdd:COG3096 508 qalaqrlqqlraqLAELEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAEleaqLEELEEQAAEAVEQRSEL 583
|
170 180
....*....|....*....|
gi 238550188 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 238550188 49 AELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKlehqyaqsykqvsvleddlsqtRAIKEQLHKYVRELEQANDDLERA 128
Cdd:COG1566 79 TDLQAALAQAEAQLAAAEAQLARLEAELGAEAEI----------------------AAAEAQLAAAQAQLDLAQRELERY 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238550188 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 238550188 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 238550188 49 AELEAQLVQAEQR-----NRDLQADNQRLKYEVEALKEKLEhQYAQSYKQvsVLEDDLSQTRAikeQLHKYVREL-EQAN 122
Cdd:pfam01442 14 EELQEQLGPVAQElvdrlEKETEALRERLQKDLEEVRAKLE-PYLEELQA--KLGQNVEELRQ---RLEPYTEELrKRLN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238550188 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 238550188 32 EARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQL 111
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 112 hKYVRELEQANDDLERAKRATIVSledfEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVT 191
Cdd:pfam02463 233 -KLNEERIDLLQELLRDEQEEIES----SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
....
gi 238550188 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 238550188 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 238550188 10 SSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEaqlvQAEQRNRDLQADNQRLKYEVEALKEkLEHQYAQ 89
Cdd:pfam05557 107 SCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKAS----EAEQLRQNLEKQQSSLAEAEQRIKE-LEFEIQS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 90 SykqvsvlEDDLSQTRAIKEQLHKYvreleqanDDLERAKRAtivsLEDFEQRLNQAIERNAFLESELDEKESLLVSVQR 169
Cdd:pfam05557 182 Q-------EQDSEIVKNSKSELARI--------PELEKELER----LREHNKHLNENIENKLLLKEEVEDLKRKLEREEK 242
|
170
....*....|..
gi 238550188 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 238550188 29 SFQEARDELVEFQEGSREleaeleAQLVQAeqrnrdlQADNQR--LKYEVEALKEKLEHqyaqsykqvsvLEDDLSQTRa 106
Cdd:pfam09738 87 SLRDIKHELKEVEEKYRK------AMISNA-------QLDNEKsnLMYQVDLLKDKLEE-----------MEESLAELQ- 141
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 238550188 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 238550188 44 SRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYkqvsvleddlSQTRAIKEQLHKYVRELEQAND 123
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQ-ALESELAISRQDYDGAT----------AQLRAAQAAVKAAQAQLAQAQI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 124 DLERAK-RATI--VSLEDF-EQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELA-----VRERQQEVTRKS 194
Cdd:pfam00529 125 DLARRRvLAPIggISRESLvTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSgaqlqIAEAEAELKLAK 204
|
....*.
gi 238550188 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 238550188 10 SSLKEETAYWKELSLK----YKQSFQEARDELVEFQEGSRELEAE--------LEAQLVQAEQRNRDLQADNQRLK---- 73
Cdd:PRK04778 201 DQLEEELAALEQIMEEipelLKELQTELPDQLQELKAGYRELVEEgyhldhldIEKEIQDLKEQIDENLALLEELDldea 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 74 -YEVEALKEKLEHQYAQ------SYKQV----SVLEDDLSQTRAIKEQLHKYVRELEQ----ANDDLERAKrativsleD 138
Cdd:PRK04778 281 eEKNEEIQERIDQLYDIlerevkARKYVeknsDTLPDFLEHAKEQNKELKEEIDRVKQsytlNESELESVR--------Q 352
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 238550188 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 238550188 9 FSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQlvqAEQRNRDLQADNQRLKyEVEALKEKLEHQYA 88
Cdd:COG5185 217 SESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQN---TDLRLEKLGENAESSK-RLNENANNLIKQFE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 89 QSYKQVSVLEDDLSQTRAIkEQLHKYVRELEqANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQ 168
Cdd:COG5185 293 NTKEKIAEYTKSIDIKKAT-ESLEEQLAAAE-AEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEV 370
|
170 180
....*....|....*....|....*.
gi 238550188 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 238550188 14 EETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVealkekLEHQYAQSYKQ 93
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE------LEQEIAALLAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 94 VSV-LEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDF-EQRLNQAIERNAFLESELDEK-ESLLVSVQRL 170
Cdd:COG4717 379 AGVeDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdEEELEEELEELEEELEELEEElEELREELAEL 458
|
170
....*....|....*....
gi 238550188 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 238550188 6 IPDFSSLKEETaywkelslkYKQSFQEARDELVEFQEGSR----------ELEAEL------EAQLVQAEQRNRDLQADN 69
Cdd:PRK04863 881 LPRLNLLADET---------LADRVEEIREQLDEAEEAKRfvqqhgnalaQLEPIVsvlqsdPEQFEQLKQDYQQAQQTQ 951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 70 QRLKYEVEALKEKLEHQYAQSYKQVsvlEDDLSQTRAIKEQLHkyvRELEQANDDLERAKRAtivsLEDFEQRLNQAIER 149
Cdd:PRK04863 952 RDAKQQAFALTEVVQRRAHFSYEDA---AEMLAKNSDLNEKLR---QRLEQAEQERTRAREQ----LRQAQAQLAQYNQV 1021
|
170 180 190
....*....|....*....|....*....|....*
gi 238550188 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 238550188 54 QLVQAEQRNRDLQADNQRLKYEVEALK--------EKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDL 125
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNnqkeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNS 354
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238550188 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 238550188 27 KQSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQ-----ADNQRlkyEVEALKEKLEHQyaqsYKQVSVLE 98
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEikrLELEIEEVEARIKKYEeqlgnVRNNK---EYEALQKEIESL----KRRISDLE 109
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 238550188 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 238550188 31 QEARDELVEFQEGSRELEAELEA--QLVQAEQRNRDLQADNQRLKYEVEALK--------EKLEHQYAQSYKQVSVLEDD 100
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRlwfaqrrlELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 101 LSQTRAIKEQLHKYVRELEQAN--------DDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQR--- 169
Cdd:COG4913 311 LERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAeaa 390
|
170 180
....*....|....*....|....*
gi 238550188 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 238550188 21 ELSLKYKQsFQEARDEL-VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQ---------- 89
Cdd:pfam07111 478 DLSLELEQ-LREERNRLdAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQlevarqgqqe 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 90 SYKQVSVLEDDLSQTRAIKEQ-LHKYVRELE-----QANDDLERAKRA------TIVSLEDFEQRLNQAIERNAFLesel 157
Cdd:pfam07111 557 STEEAASLRQELTQQQEIYGQaLQEKVAEVEtrlreQLSDTKRRLNEArreqakAVVSLRQIQHRATQEKERNQEL---- 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 158 dekesllvsvQRLKDEARDLRQELAVReRQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENSFPSPKAIPN 237
Cdd:pfam07111 633 ----------RRLQDEARKEEGQRLAR-RVQELERDKNLMLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECS 701
|
250
....*....|....
gi 238550188 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 238550188 41 QEGSRELEAELEAQLVQAEQRNRDlqadnqrlKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQ 120
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKE--------KERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238550188 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 238550188 13 KEEtayWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKY---EVEALKEKLEHQYAq 89
Cdd:PRK12704 63 KEE---IHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQkqqELEKKEEELEELIE- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 90 syKQVSVLED--DLSQTRAiKEQLhkyvreLEQANDDLERAKRATIvsledfeqrlnQAIERNAFLESELDEKESLLVSV 167
Cdd:PRK12704 139 --EQLQELERisGLTAEEA-KEIL------LEKVEEEARHEAAVLI-----------KEIEEEAKEEADKKAKEILAQAI 198
|
....*.
gi 238550188 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 238550188 20 KELSLKYKQSFQEARDELVEFQEGSRELEaELEAQLVQAEQRNRDLQADNQRLKYE-VEALKEKLEhQYAQSYKQVSVLE 98
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKLA-ELEKKLDELEEELAELLKELEELGFEsVEELEERLK-ELEPFYNEYLELK 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 99 DDLSQTRAIKEQLHKYVRELEQANDDLERAKRA------------TIVSLEDFEQRLNQAIERNAFLESELDEKESLLVS 166
Cdd:PRK03918 609 DAEKELEREEKELKKLEEELDKAFEELAETEKRleelrkeleeleKKYSEEEYEELREEYLELSRELAGLRAELEELEKR 688
|
170 180
....*....|....*....|...
gi 238550188 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 238550188 28 QSFQEARDELVEFQEgsrELEAElEAQLVQAEQRNRDLQAdnqrlkyEVEALKEKLEhqyaqsykqvsvleDDLSQTRAI 107
Cdd:pfam01576 264 KKIRELEAQISELQE---DLESE-RAARNKAEKQRRDLGE-------ELEALKTELE--------------DTLDTTAAQ 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 108 KEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIER-NAFLESELDEKESLLVSVQRLKDEARDLRQEL-AVRE 185
Cdd:pfam01576 319 QELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEElTEQLEQAKRNKANLEKAKQALESENAELQAELrTLQQ 398
|
....*...
gi 238550188 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 238550188 27 KQSFQEARDELVEFQEGSRELEAELEA----------QLVQAEQRNRDLQADNQRLKYEVEAL---KEKLEHQYAQSYKQ 93
Cdd:COG4372 65 EEELEQARSELEQLEEELEELNEQLQAaqaelaqaqeELESLQEEAEELQEELEELQKERQDLeqqRKQLEAQIAELQSE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 94 VSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVsledfeQRLNQAIERNAFLESELDEKESLLVSVQRLKDE 173
Cdd:COG4372 145 IAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL------DELLKEANRNAEKEEELAEAEKLIESLPRELAE 218
|
....*.
gi 238550188 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 238550188 8 DFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELE---AELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLE 84
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSeelADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 238550188 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 238550188 41 QEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHkyvRELEQ 120
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEEL---LEEEE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 121 ANDDLERAKRATIVSLEDFEQRLNQ--------------AIE-------RNAFLESELD----EKESLLVSVQRLKDEAR 175
Cdd:COG1196 747 LLEEEALEELPEPPDLEELERELERlereiealgpvnllAIEeyeeleeRYDFLSEQREdleeARETLEEAIEEIDRETR 826
|
..
gi 238550188 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 238550188 32 EARDELVEFQEGSRELEAELEAQlVQAEQRNRDLQADNQRL----------KYEVEALKEKLEHQYAQSYKQVSVLEDDL 101
Cdd:pfam01576 630 EAREKETRALSLARALEEALEAK-EELERTNKQLRAEMEDLvsskddvgknVHELERSKRALEQQVEEMKTQLEELEDEL 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 102 SQTRAIKEQLH--------KYVRELeQANDDLERAKRATIVS--------LEDFEQRLNQAIERNAFLESELDEKESLLV 165
Cdd:pfam01576 709 QATEDAKLRLEvnmqalkaQFERDL-QARDEQGEEKRRQLVKqvreleaeLEDERKQRAQAVAAKKKLELDLKELEAQID 787
|
170 180 190
....*....|....*....|....*....|...
gi 238550188 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 238550188 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 238550188 34 RDELVEFQEGSRELEAELEAQLvqaEQRNRDLQADNQRLKYEVEALKEKLEhqyaqsykQVSVLEDDLSQTRAIKEQLHK 113
Cdd:PRK12704 56 KEALLEAKEEIHKLRNEFEKEL---RERRNELQKLEKRLLQKEENLDRKLE--------LLEKREEELEKKEKELEQKQQ 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238550188 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 238550188 28 QSFQEARDELVEFqEGSRELEAELEAQLVQAEQR-NRDLQ--ADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQT 104
Cdd:PRK04863 513 EQLQQLRMRLSEL-EQRLRQQQRAERLLAEFCKRlGKNLDdeDELEQLQEELEARLESLSESVSEARERRMALRQQLEQL 591
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 238550188 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 238550188 49 AELEAQLVQAEQRNRDLQADNQRLKYEVEALkeklehqyaQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERA 128
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGLVDLSEEAK---------LLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 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 238550188 38 VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEhQYAQSYKQVSVLEDDLSQTRaikeqlhkyVRE 117
Cdd:COG3096 828 VAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQ-LLNKLLPQANLLADETLADR---------LEE 897
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238550188 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 238550188 13 KEETAYwkELSLKYKQSFQEARDELVEFQEGSRELE---AELEAQLVQAEQRNRDLQADNQRLKYEVEALK--------- 80
Cdd:PRK03918 159 DYENAY--KNLGEVIKEIKRRIERLEKFIKRTENIEeliKEKEKELEEVLREINEISSELPELREELEKLEkevkeleel 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 81 ----EKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLE--RAKRATIVSLEDFEQRLNQAIERnafLE 154
Cdd:PRK03918 237 keeiEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELRE---IE 313
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 238550188 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 238550188 28 QSFQEARDELVEF--QEGSRELEAELEAQLVQAEQRNRDLQadnqrlkyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTR 105
Cdd:COG3096 492 QAWQTARELLRRYrsQQALAQRLQQLRAQLAELEQRLRQQQ--------NAERLLEEFCQRIGQQLDAAEELEELLAELE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 106 AIKEQLHKYVRELEQANDDLER---AKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQrlkdearDLRQELA 182
Cdd:COG3096 564 AQLEELEEQAAEAVEQRSELRQqleQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVT-------AAMQQLL 636
|
170
....*....|
gi 238550188 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 238550188 11 SLKEETAYWKElSLKYK--------QSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQrlkyevEALKEk 82
Cdd:TIGR00618 687 SEKEQLTYWKE-MLAQCqtllreleTHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQAR------TVLKA- 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 83 LEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLN----QAIERNAFLESELD 158
Cdd:TIGR00618 759 RTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNlqceTLVQEEEQFLSRLE 838
|
170 180 190
....*....|....*....|....*....|
gi 238550188 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 238550188 35 DELVEFQEGSRELEAELEAQLVQAEQRNRD-LQADNQRLKYEVEALKEKLEHQYAQsYKQVSVLEDDLSQTRAIKEQLHK 113
Cdd:pfam12128 397 DKLAKIREARDRQLAVAEDDLQALESELREqLEAGKLEFNEEEYRLKSRLGELKLR-LNQATATPELLLQLENFDERIER 475
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238550188 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 238550188 33 ARDELVEFQEGSRELEaELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEhqyaQSYKQVSVLEDDLSQTRAIKEQLH 112
Cdd:TIGR02169 669 SRSEPAELQRLRERLE-GLKRELSSLQSELRRIENRLDELSQELSDASRKIG----EIEKEIEQLEQEEEKLKERLEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 113 KYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKEsllvsVQRLKDEARDL-----RQELAVRERQ 187
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSR-----IPEIQAELSKLeeevsRIEARLREIE 818
|
....*..
gi 238550188 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 238550188 12 LKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAqlVQAEQRNRDLQADN----QRLKYEVEALKEKLEHQY 87
Cdd:pfam15294 131 LHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKD--LQKEQGAKKDVKSNlkeiSDLEEKMAALKSDLEKTL 208
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 238550188 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 238550188 98 EDDLSQTRAIKEQLHKYVRELEQANDDLERA---------KRATIVSLEDFEQRlnqAIERNAF-LESELDEKESLLVSV 167
Cdd:pfam15898 7 EEELQENERLKRKLQDAQQELAELKSQLERLtqqrqesfsDRSSLLETEKREKR---ALERKISeMEEELKVLEDLRAEN 83
|
90
....*....|
gi 238550188 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 238550188 26 YKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRnrDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLeDDLSQTR 105
Cdd:PRK02224 167 YRERASDARLGVERVLSDQRGSLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARETR-DEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 106 AIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLvSVQRLKDEARDLRQElAVRE 185
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA-GLDDADAEAVEARRE-ELED 321
|
....*..
gi 238550188 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 238550188 32 EARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEhqyaqsykqvsVLEDDLSQTRAIKEQL 111
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE-----------ELEEKVKELKELKEKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 112 HKYvRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLES------ELDEKES-LLVSVQRLKDEARDLRQELAVR 184
Cdd:PRK03918 293 EEY-IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeerleELKKKLKeLEKRLEELEERHELYEEAKAKK 371
|
170
....*....|....*
gi 238550188 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 238550188 65 LQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHK-------------YVRELEQANDDLERAkRA 131
Cdd:COG4913 604 LGFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvasAEREIAELEAELERL-DA 682
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238550188 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 238550188 4 EDIPDFSSLKEETAYWKELSLKYK-QSFQEARDELveFQEGSRELEAELEAQLVQAEQRN---RDLQADNQRLKYEVEAL 79
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELQlEELEQEIAAL--LAEAGVEDEEELRAALEQAEEYQelkEELEELEEQLEELLGEL 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 80 KEKLE-HQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRativsLEDFEQRLNQAIERNAFLESELD 158
Cdd:COG4717 419 EELLEaLDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE-----LAELLQELEELKAELRELAEEWA 493
|
170 180
....*....|....*....|.
gi 238550188 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 238550188 28 QSFQEARDELVEFQEGSRELEaELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYA--QSYKQVSVleDDLSQTR 105
Cdd:PRK14146 23 QTLEESKLENMNSEESQTITE-ETQEQAVEGAETETSLQKELDNAKKEIESLKDSWARERAefQNFKRRSA--QEFVSIR 99
|
90 100
....*....|....*....|..
gi 238550188 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 238550188 31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKqvsvLEDDLSQTRAIKEQ 110
Cdd:pfam01576 60 EEMRARLAARKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQK----LQLEKVTTEAKIKK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 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 238550188 36 ELVEFQEGSRELEAELEA--QLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQyAQSYKQVSVLEDDLSQTRAI-KEQLH 112
Cdd:cd00176 1 KLQQFLRDADELEAWLSEkeELLSSTDYGDDLESVEALLK-KHEALEAELAAH-EERVEALNELGEQLIEEGHPdAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238550188 113 KYVRELEQANDDLERAkrativsLEDFEQRLNQAIERNAF------LESELDEKESLLVS---------VQRLKDEARDL 177
Cdd:cd00176 79 ERLEELNQRWEELREL-------AEERRQRLEEALDLQQFfrdaddLEQWLEEKEAALASedlgkdlesVEELLKKHKEL 151
|
....*...
gi 238550188 178 RQELAVRE 185
Cdd:cd00176 152 EEELEAHE 159
|
|
| |
