|
Name |
Accession |
Description |
Interval |
E-value |
| NUDE_C |
pfam04880 |
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ... |
135-309 |
2.10e-58 |
|
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: 185.76 E-value: 2.10e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 135 SLEDFEQRLNQAIERNAFLESEL----DEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSP---TLDCEKMD 207
Cdd:pfam04880 1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKLRNLLMRSPSTPslqTLEIFDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 208 SAVQASlslpATPVG-KGTENTFPSpkAIPNGFGTSPLTPSARISAlnivgDLLRKVGALESKLAACRNFAKDQASRKSY 286
Cdd:pfam04880 81 PAVQAV----SSPVIaTPPEKSFNS--LRTGSETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNASRRG 149
|
170 180
....*....|....*....|...
gi 71284108 287 isgNVNCGVLNGNGTKFSRSGHT 309
Cdd:pfam04880 150 ---NSRSLYGSRPPTKFAHSRHT 169
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-195 |
4.90e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 27 KQSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAqsykQVSVLEDDLSQ 103
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEEELAELEEELEELEE----ELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 104 TRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAV 183
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
170
....*....|..
gi 71284108 184 RERQQEVTRKSA 195
Cdd:COG1196 429 ALAELEEEEEEE 440
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
27-188 |
1.55e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 27 KQSFQEARDELVEFQEGSRELEaELEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQS-YKQVSVLEDDLS 102
Cdd:COG4913 270 RLAELEYLRAALRLWFAQRRLE-LLEAELEELRAELARLEAELERLEARLDALREEldeLEAQIRGNgGDRLEQLEREIE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 103 QTRAIKEQLhkyVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKE----SLLVSVQRLKDEARDLR 178
Cdd:COG4913 349 RLERELEER---ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEealaEAEAALRDLRRELRELE 425
|
170
....*....|
gi 71284108 179 QELAVRERQQ 188
Cdd:COG4913 426 AEIASLERRK 435
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
13-192 |
1.99e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 13 KEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQ 89
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyeLLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 90 SYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQR 169
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180
....*....|....*....|....*...
gi 71284108 170 LKDEARD-----LRQELAVRERQQEVTR 192
Cdd:COG1196 380 ELEELAEelleaLRAAAELAAQLEELEE 407
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
24-195 |
2.23e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.45 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 24 LKYKQSFQEARDELVEFQEGSRELEAELEA---QLVQAEQRNRDLQADNQRLKYEVEALKEklehQYAQSYKQVSVLEDD 100
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAElrkELEELEEELEQLRKELEELSRQISALRK----DLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 101 LSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESllvSVQRLKDEARDLRQE 180
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANLRER 825
|
170
....*....|....*
gi 71284108 181 LAVRERQQEVTRKSA 195
Cdd:TIGR02168 826 LESLERRIAATERRL 840
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-193 |
7.01e-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: 53.91 E-value: 7.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 27 KQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRA 106
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 107 IKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLvsvQRLKDEARDLRQELAVRER 186
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI---EELESELEALLNERASLEE 887
|
....*..
gi 71284108 187 QQEVTRK 193
Cdd:TIGR02168 888 ALALLRS 894
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
27-193 |
1.87e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 27 KQSFQEARDELVEFQEGSRELEaELEAQLVQAEQRNRDLQADNQRLKYEVEAL-----KEKLEHQYAQSYKQVSVLEDDL 101
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLLQLLplyqeLEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 102 SQTRAIKEQLHKYVRELEQANDDLERAKRATivsLEDFEQRLNQAIERNAFLESELDEKESLLvsvQRLKDEARDLRQEL 181
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQL---SLATEEELQDLAEELEELQQRLAELEEEL---EEAQEELEELEEEL 229
|
170
....*....|..
gi 71284108 182 AVRERQQEVTRK 193
Cdd:COG4717 230 EQLENELEAAAL 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
45-192 |
1.95e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 45 RELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHqyAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDD 124
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREA--LQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 125 LERAKR---ATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDL------------RQELAVRERQQE 189
Cdd:COG4913 687 LAALEEqleELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelralleerFAAALGDAVERE 766
|
...
gi 71284108 190 VTR 192
Cdd:COG4913 767 LRE 769
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
31-189 |
2.17e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQ 110
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA-EAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71284108 111 LhkyVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQE 189
Cdd:COG1196 412 L---LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
31-258 |
4.12e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYaQSYKQVSVLE------------ 98
Cdd:COG3883 40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY-RSGGSVSYLDvllgsesfsdfl 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 99 DDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLR 178
Cdd:COG3883 119 DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 179 QELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENTFPSPKAIPNGFGTSPLTPSARISALNIVGD 258
Cdd:COG3883 199 AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAA 278
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
10-199 |
8.32e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 8.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 10 SSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEA---ELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQ 86
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 87 YAQSYK--QVSVLE-----DDLSQT-------RAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAF 152
Cdd:COG4942 110 LRALYRlgRQPPLAlllspEDFLDAvrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 71284108 153 LESELDEKESLLVSVQR-----------LKDEARDLRQELAVRERQQEVTRKSAPSSP 199
Cdd:COG4942 190 LEALKAERQKLLARLEKelaelaaelaeLQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
8-202 |
9.39e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 9.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 8 DFSSLKEETAYWkELSLKYKqsfqEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQY 87
Cdd:TIGR02169 215 ALLKEKREYEGY-ELLKEKE----ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 88 AQSYKQVSVLEDDLSQTRAIKEQLHKYVRELE--QANDDLERakRATIVSLEDFEQRLNQAIERNAFLESELDEK----E 161
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLERSIAEKERELEDAEerLAKLEAEI--DKLLAEIEELEREIEEERKRRDKLTEEYAELkeelE 367
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 71284108 162 SLLVSVQRLKDEARDLRQELA-VRERQQEVTRKSAPSSPTLD 202
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKdYREKLEKLKREINELKRELD 409
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
28-195 |
1.44e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 28 QSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQT 104
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEElaeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 105 RAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVR 184
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
170
....*....|.
gi 71284108 185 ERQQEVTRKSA 195
Cdd:COG1196 462 LELLAELLEEA 472
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
20-193 |
2.42e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 20 KELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQaeqrnrdLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLED 99
Cdd:TIGR02168 227 LALLVLRLEELREELEELQEELKEAEEELEELTAELQE-------LEEKLEELRLEVSELEEEIEELQKELYALANEISR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 100 DLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDF---EQRLNQAIERNAFLESELDEKESLLV----SVQRLKD 172
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELaelEEKLEELKEELESLEAELEELEAELEelesRLEELEE 379
|
170 180
....*....|....*....|.
gi 71284108 173 EARDLRQELAVRERQQEVTRK 193
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNN 400
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
39-195 |
2.59e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 39 EFQEGSRELEAELeaQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVREL 118
Cdd:COG1196 217 ELKEELKELEAEL--LLLKLRELEAELEELEAELE-ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71284108 119 EQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSA 195
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-177 |
3.29e-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: 48.90 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 4 EDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQ---LVQAEQRNRDLQADNQRLKYEVEALK 80
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLrskVAQLELQIASLNNEIERLEARLERLE 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 81 --------EKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAF 152
Cdd:TIGR02168 414 drrerlqqEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
170 180
....*....|....*....|....*
gi 71284108 153 LESELDEKESLLVSVQRLKDEARDL 177
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSGL 518
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
10-195 |
1.21e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 10 SSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQ------ADNQRLKYEVEALKEKL 83
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSsleqeiENVKSELKELEARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 84 EHQYAQSYKQVSVLEDDLSQTRaikeqlhkyVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESL 163
Cdd:TIGR02169 771 EEDLHKLEEALNDLEARLSHSR---------IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
170 180 190
....*....|....*....|....*....|....
gi 71284108 164 LVSVQRLKDEARDLRQEL--AVRERQQEVTRKSA 195
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLngKKEELEEELEELEA 875
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-189 |
1.35e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 25 KYKQSFQEARDELVEFQEGSRELEAELEA---QLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDL 101
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 102 SQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDF---EQRLNQAIERNAFLESELDEKESllvSVQRLKDEARDLR 178
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERaslEEALALLRSELEELSEELRELES---KRSELRRELEELR 921
|
170
....*....|..
gi 71284108 179 QELA-VRERQQE 189
Cdd:TIGR02168 922 EKLAqLELRLEG 933
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
31-196 |
1.79e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEq 110
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-DLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 111 LHKYVRELEQA---NDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKEsllvsvQRLKDEARDLRQELAVRERQ 187
Cdd:COG1579 91 YEALQKEIESLkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK------AELDEELAELEAELEELEAE 164
|
....*....
gi 71284108 188 QEVTRKSAP 196
Cdd:COG1579 165 REELAAKIP 173
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
31-182 |
3.05e-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: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALK---EKLEHQYAQSYKQVSVLEDDLSQTRAI 107
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEeliEELESELEALLNERASLEEALALLRSE 895
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 108 KEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLV------------SVQRLKDEAR 175
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLeeaealenkiedDEEEARRRLK 975
|
....*..
gi 71284108 176 DLRQELA 182
Cdd:TIGR02168 976 RLENKIK 982
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
22-149 |
7.92e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 22 LSLKyKQSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKekleHQYAQSYKQVSVLE 98
Cdd:PRK09039 69 LSLE-RQGNQDLQDSVANLRASLSAAEAErsrLQALLAELAGAGAAAEGRAGELAQELDSEK----QVSARALAQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 71284108 99 DDLSqtrAIKEQLHKyvreLEQANDDLERAKRATIVSLEDFEQRLNQAIER 149
Cdd:PRK09039 144 QQIA---ALRRQLAA----LEAALDASEKRDRESQAKIADLGRRLNVALAQ 187
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-195 |
8.96e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 30 FQEARDELVEFQE---GSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQ---YAQSYKQVSVLEDDLSQ 103
Cdd:TIGR02168 276 VSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEELKEELES 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 104 TRAIKEQLHKYVRELEQANDDLERAkrativsLEDFEQRLNQAIERNAFLESELdekESLLVSVQRLKDEARDLRQELAV 183
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQ-------LETLRSKVAQLELQIASLNNEI---ERLEARLERLEDRRERLQQEIEE 425
|
170
....*....|..
gi 71284108 184 RERQQEVTRKSA 195
Cdd:TIGR02168 426 LLKKLEEAELKE 437
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
12-189 |
9.37e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 12 LKEETAYWKELSLKYKQSFQEARDELVEFqegsRELEAELEAQLVQAEQrnrdlQADNQRLKYevealkEKLEHQYAQSY 91
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEEL----EAELEELESRLEELEE-----QLETLRSKV------AQLELQIASLN 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 92 KQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVS-----LEDFEQRLNQAIERNAFLESELDEKESLLVS 166
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEeleeeLEELQEELERLEEALEELREELEEAEQALDA 479
|
170 180
....*....|....*....|...
gi 71284108 167 vqrLKDEARDLRQELAVRERQQE 189
Cdd:TIGR02168 480 ---AERELAQLQARLDSLERLQE 499
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
50-192 |
1.21e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 50 ELEAQLVQAEQRNRDLQADNQRLKY---EVEALKEKLEH--QYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQAndd 124
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEEleeELEELEAELEElrEELEKLEKLLQLLPLYQELEALEAELAELPERLEEL--- 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 125 leRAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLV--SVQRLKDEARDLRQELAVRERQQEVTR 192
Cdd:COG4717 152 --EERLEELRELEEELEELEAELAELQEELEELLEQLSLATeeELQDLAEELEELQQRLAELEEELEEAQ 219
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
27-183 |
1.27e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 27 KQSFQEARDELVEFQEGSRELEAELEA-----QLVQAEQRnrdLQADNQRLKYEVEALKEKLEHQ---YAQSYKQVSVLE 98
Cdd:COG3096 305 QYRLVEMARELEELSARESDLEQDYQAasdhlNLVQTALR---QQEKIERYQEDLEELTERLEEQeevVEEAAEQLAEAE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 99 DDLSQTRA----IKEQLHKYVRELE----------QANDDLERAKR---ATIVSLEDFEQRLnqaiernafleSELDEKE 161
Cdd:COG3096 382 ARLEAAEEevdsLKSQLADYQQALDvqqtraiqyqQAVQALEKARAlcgLPDLTPENAEDYL-----------AAFRAKE 450
|
170 180
....*....|....*....|..
gi 71284108 162 sllvsvQRLKDEARDLRQELAV 183
Cdd:COG3096 451 ------QQATEEVLELEQKLSV 466
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
27-192 |
1.40e-04 |
|
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: 43.67 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 27 KQSFQEARDEL----VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKE-----KLEHQYA-QSYKQV-- 94
Cdd:pfam12128 645 RTALKNARLDLrrlfDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEeqkeqKREARTEkQAYWQVve 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 95 ---SVLEDDLSQTRAIKEQLHK---------YVREL------EQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESE 156
Cdd:pfam12128 725 galDAQLALLKAAIAARRSGAKaelkaletwYKRDLaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQET 804
|
170 180 190
....*....|....*....|....*....|....*..
gi 71284108 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 |
1.64e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 12 LKEETAYWKElslkYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALK----------E 81
Cdd:TIGR02169 838 LQEQRIDLKE----QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELErkieeleaqiE 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 82 KLEHQYAQSYKQVSVLEDDLSQTRAIK-------------EQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIE 148
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELSEIEDPKgedeeipeeelslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE 993
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71284108 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 |
2.59e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 2.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 24 LKYKQSFQEARDELVEFQEGSRELE---AELEAQLV----QAE--QRNRDLQADNQRLK-----YEVEALKEKLEH---Q 86
Cdd:TIGR02168 168 SKYKERRKETERKLERTRENLDRLEdilNELERQLKslerQAEkaERYKELKAELRELElallvLRLEELREELEElqeE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 87 YAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVS 166
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190
....*....|....*....|....*....|
gi 71284108 167 VQRLKDEARDLRQELAVRERQQEVTRKSAP 196
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLE 357
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
25-198 |
3.36e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 25 KYKQSFQEARDELVEFQEGSRELEAELEA-----QLVQAEQRNRDLQADNQRLKYEVEALKEKLEH-------------- 85
Cdd:COG3206 186 ELRKELEEAEAALEEFRQKNGLVDLSEEAklllqQLSELESQLAEARAELAEAEARLAALRAQLGSgpdalpellqspvi 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 86 -QYAQSYKQVSVLEDDLSQT--------RAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESE 156
Cdd:COG3206 266 qQLRAQLAELEAELAELSARytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE 345
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 71284108 157 LDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSS 198
Cdd:COG3206 346 LPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
|
| PRK13922 |
PRK13922 |
rod shape-determining protein MreC; Provisional |
143-189 |
8.55e-04 |
|
rod shape-determining protein MreC; Provisional
Pssm-ID: 237560 Cd Length: 276 Bit Score: 40.35 E-value: 8.55e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 71284108 143 LNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQE 189
Cdd:PRK13922 71 LFDLREENEELKKELLELESRLQELEQLEAENARLRELLNLKESLDY 117
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
38-187 |
8.95e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 38 VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALK--EKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYV 115
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDriERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 116 RELE--------QANDDLERA--KRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLkdeaRDLRQELAVRE 185
Cdd:PRK02224 547 AELEaeaeekreAAAEAEEEAeeAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERL----REKREALAELN 622
|
..
gi 71284108 186 RQ 187
Cdd:PRK02224 623 DE 624
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
35-189 |
9.03e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 9.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 35 DELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQrlkyevealkeklehQYAQSYKQVSVLEDDLSQTRAIK------ 108
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHS---------------QFEQAYQLVRKIAGEVSRSEAWDvarell 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 109 -------------EQLHKYVRELEQANDDLERAKRAtivsLEDFEQRLNQAIERNAFLESELDEKESLLVSvqrLKDEAR 175
Cdd:PRK04863 503 rrlreqrhlaeqlQQLRMRLSELEQRLRQQQRAERL----LAEFCKRLGKNLDDEDELEQLQEELEARLES---LSESVS 575
|
170
....*....|....
gi 71284108 176 DLRQELAVRERQQE 189
Cdd:PRK04863 576 EARERRMALRQQLE 589
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
41-194 |
1.10e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 41 QEGSRELEAELEaQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRA----IKEQLHKYVR 116
Cdd:COG4942 19 ADAAAEAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAelaeLEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 117 ELEQANDDLERAKRAT-----------IVSLEDFEQ--RLNQAIER-NAFLESELDEKESLLVSVQRLKDEARDLRQELA 182
Cdd:COG4942 98 ELEAQKEELAELLRALyrlgrqpplalLLSPEDFLDavRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170
....*....|..
gi 71284108 183 VRERQQEVTRKS 194
Cdd:COG4942 178 ALLAELEEERAA 189
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
49-190 |
1.19e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.03 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 49 AELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKlehqyaqsykqvsvleddlsqtRAIKEQLHKYVRELEQANDDLERA 128
Cdd:COG1566 79 TDLQAALAQAEAQLAAAEAQLARLEAELGAEAEI----------------------AAAEAQLAAAQAQLDLAQRELERY 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71284108 129 KRAT---IVSLEDFEQRLNQAIErnafLESELDEKESLLVSVQRLKDEARDLRQ-ELAVRERQQEV 190
Cdd:COG1566 137 QALYkkgAVSQQELDEARAALDA----AQAQLEAAQAQLAQAQAGLREEEELAAaQAQVAQAEAAL 198
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
31-148 |
1.27e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 31 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQAdnqrLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQT--RAIK 108
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEA----LLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqQAIK 580
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 71284108 109 E------QLHKYVRELEQANDDLERAKRativsLEDFEQRLNQAIE 148
Cdd:PRK00409 581 EakkeadEIIKELRQLQKGGYASVKAHE-----LIEARKRLNKANE 621
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
31-182 |
1.33e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 31 QEARDELVEFQEGSRELEA------ELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQ--------SYKQVSV 96
Cdd:COG4913 671 AELEAELERLDASSDDLAAleeqleELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaedlaRLELRAL 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 97 LEDDLSQ----------TRAIKEQLHKYVRELEQANDDLERAKR--------------ATIVSLEDFEQRLNQAIE---- 148
Cdd:COG4913 751 LEERFAAalgdaverelRENLEERIDALRARLNRAEEELERAMRafnrewpaetadldADLESLPEYLALLDRLEEdglp 830
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 71284108 149 ------RNAFLESELDEKESLLvsvQRLKDEARDLRQELA 182
Cdd:COG4913 831 eyeerfKELLNENSIEFVADLL---SKLRRAIREIKERID 867
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
12-190 |
1.36e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 12 LKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQlvqaeQRNRDLQADNQRLKYEVEALKEKLEH------ 85
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-----ERIRTLLAAIADAEDEIERLREKREAlaelnd 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 86 ----QYAQSYKQVSVLEDD-----LSQTRAIKEQLHKYVRELEQANDDLERAK---RATIVSLEDFEQRLNQAIERNAFL 153
Cdd:PRK02224 624 erreRLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERddlQAEIGAVENELEELEELRERREAL 703
|
170 180 190
....*....|....*....|....*....|....*..
gi 71284108 154 ESELDEKESLLVSVQRLKDEARDLRQELavreRQQEV 190
Cdd:PRK02224 704 ENRVEALEALYDEAEELESMYGDLRAEL----RQRNV 736
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
20-193 |
1.38e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 20 KELSLKYKQSFQEARDELVEFQEGSRELEAEL---------EAQLVQAEQRNRDLQADNQRLK-YEVEALK------EKL 83
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELrelekvlkkESELIKLKELAEQLKELEEKLKkYNLEELEkkaeeyEKL 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 84 EHQYAQSYKQVSVLEDDL-------SQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESE 156
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELekleelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDA 610
|
170 180 190
....*....|....*....|....*....|....*..
gi 71284108 157 LDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRK 193
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
32-180 |
1.40e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 32 EARDELV---EFQEGSRE----LEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQSYKQVSVLEDDL 101
Cdd:PRK02224 293 EERDDLLaeaGLDDADAEaveaRREELEDRDEELRDRLEECRVAAQAHNEEAESLREDaddLEERAEELREEAAELESEL 372
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71284108 102 SQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQE 180
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
41-196 |
1.57e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 41 QEGSRELEAELEAQLVQAEQRNRDLQadnQRLkyeveALKEKLEHQYAQSYKQVSVLEDDLSQTRA---IKEQLHKY--- 114
Cdd:COG3096 436 PENAEDYLAAFRAKEQQATEEVLELE---QKL-----SVADAARRQFEKAYELVCKIAGEVERSQAwqtARELLRRYrsq 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 115 -------------VRELEQANDDLERAKRativSLEDFEQRLNQAIERNAFLESELDE----KESLLVSVQRLKDEARDL 177
Cdd:COG3096 508 qalaqrlqqlraqLAELEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAEleaqLEELEEQAAEAVEQRSEL 583
|
170 180
....*....|....*....|
gi 71284108 178 RQEL-AVRERQQEVTRKsAP 196
Cdd:COG3096 584 RQQLeQLRARIKELAAR-AP 602
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
32-212 |
1.86e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 32 EARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQSYKQVSVLEDDLSQTR 105
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEvsrIEARLREIEQKLNRLTLEKEYLEKEIQELQEQridLKEQIKSIEKEIENLNGKKEELE 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 106 AIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQaiernafLESELDEKESLLvsvQRLKDEARDLRQELAVRE 185
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-------LEAQIEKKRKRL---SELKAKLEALEEELSEIE 937
|
170 180
....*....|....*....|....*..
gi 71284108 186 RqqEVTRKSAPSSPTLDCEKMDSAVQA 212
Cdd:TIGR02169 938 D--PKGEDEEIPEEELSLEDVQAELQR 962
|
|
| FtsB |
COG2919 |
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning]; |
49-84 |
2.07e-03 |
|
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442163 [Multi-domain] Cd Length: 96 Bit Score: 36.78 E-value: 2.07e-03
10 20 30
....*....|....*....|....*....|....*.
gi 71284108 49 AELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLE 84
Cdd:COG2919 32 RELRQEIAELEAENAKLKARNAELEAEVADLKDGPD 67
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
25-189 |
2.28e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 39.69 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 25 KYKQSFQEARDELVEFQEGSREL--EAELEAQLVQAEQRNRDLQADNQRlkyevealKEKLEHQYAQSYKQvsvleddls 102
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKleAALLEAKELLLRERNQQRQEARRE--------REELQREEERLVQK--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 103 qtraiKEQLHKYVRELEQANDDLERAKRAtivsledFEQRLNQAIERNAFLESELDEKESLLVSVQR---LKDEARDLRQ 179
Cdd:PRK12705 90 -----EEQLDARAEKLDNLENQLEEREKA-------LSARELELEELEKQLDNELYRVAGLTPEQARkllLKLLDAELEE 157
|
170
....*....|
gi 71284108 180 ELAVRERQQE 189
Cdd:PRK12705 158 EKAQRVKKIE 167
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
44-200 |
2.45e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 39.33 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 44 SRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYkqvsvleddlSQTRAIKEQLHKYVRELEQAND 123
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQ-ALESELAISRQDYDGAT----------AQLRAAQAAVKAAQAQLAQAQI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 124 DLERAK-RATI--VSLEDF-EQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELA-----VRERQQEVTRKS 194
Cdd:pfam00529 125 DLARRRvLAPIggISRESLvTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSgaqlqIAEAEAELKLAK 204
|
....*.
gi 71284108 195 APSSPT 200
Cdd:pfam00529 205 LDLERT 210
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
12-211 |
3.82e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.18 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 12 LKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELE-----AELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQ 86
Cdd:TIGR00618 251 AQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaAPLAAHIKAVTQIEQQAQRIHTELQ-SKMRSRAKLLMK 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 87 YAQSYKQvsvlEDDLSQTRAIKEQLHKYVRELEQANDD----LERAKRATIVS--LEDFEQRLNQAIERNAFLESELDEK 160
Cdd:TIGR00618 330 RAAHVKQ----QSSIEEQRRLLQTLHSQEIHIRDAHEVatsiREISCQQHTLTqhIHTLQQQKTTLTQKLQSLCKELDIL 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 71284108 161 ESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAP-----SSPTLDCEKMDSAVQ 211
Cdd:TIGR00618 406 QREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAElcaaaITCTAQCEKLEKIHL 461
|
|
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
29-154 |
3.99e-03 |
|
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.
Pssm-ID: 462869 [Multi-domain] Cd Length: 303 Bit Score: 38.52 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 29 SFQEARDELVEFQEGSREleaeleAQLVQAeqrnrdlQADNQR--LKYEVEALKEKLEHqyaqsykqvsvLEDDLSQTRa 106
Cdd:pfam09738 87 SLRDIKHELKEVEEKYRK------AMISNA-------QLDNEKsnLMYQVDLLKDKLEE-----------MEESLAELQ- 141
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 71284108 107 ikeqlhkyvRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLE 154
Cdd:pfam09738 142 ---------RELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIE 180
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
12-183 |
4.20e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 38.93 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 12 LKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSY 91
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 92 KQVSVLeddLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDfeqrLNQAIERNAFLESELdekESLLVSVQRLK 171
Cdd:pfam05483 240 KQVSLL---LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDEN----LKELIEKKDHLTKEL---EDIKMSLQRSM 309
|
170
....*....|..
gi 71284108 172 DEARDLRQELAV 183
Cdd:pfam05483 310 STQKALEEDLQI 321
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
6-184 |
4.69e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 38.78 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 6 IPDFSSLKEETaywkelslkYKQSFQEARDELVEFQEGSR----------ELEAEL------EAQLVQAEQRNRDLQADN 69
Cdd:PRK04863 881 LPRLNLLADET---------LADRVEEIREQLDEAEEAKRfvqqhgnalaQLEPIVsvlqsdPEQFEQLKQDYQQAQQTQ 951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 70 QRLKYEVEALKEKLEHQYAQSYKQVsvlEDDLSQTRAIKEQLHkyvRELEQANDDLERAKRAtivsLEDFEQRLNQAIER 149
Cdd:PRK04863 952 RDAKQQAFALTEVVQRRAHFSYEDA---AEMLAKNSDLNEKLR---QRLEQAEQERTRAREQ----LRQAQAQLAQYNQV 1021
|
170 180 190
....*....|....*....|....*....|....*
gi 71284108 150 NAFLESELDEKEsllvsvQRLKDEARDLrQELAVR 184
Cdd:PRK04863 1022 LASLKSSYDAKR------QMLQELKQEL-QDLGVP 1049
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
41-195 |
5.29e-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: 38.34 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 41 QEGSRELEAELEAQLVQAEQRNRDlqadnqrlKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQ 120
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKE--------KERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71284108 121 ANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLvsvQRLKDeardlRQELAVRERQQEVTRKSA 195
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETEL---ERMKE-----RAKKAGAQRKEEEAERKQ 175
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
45-147 |
5.76e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 37.19 E-value: 5.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 45 RELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQyaQSYKQvsvledDLSQTRAIKEQLHKYVRELEQANDD 124
Cdd:pfam13851 39 KKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENY--EKDKQ------SLKNLKARLKVLEKELKDLKWEHEV 110
|
90 100
....*....|....*....|...
gi 71284108 125 LERAKRATIVSLEDFEQRLNQAI 147
Cdd:pfam13851 111 LEQRFEKVERERDELYDKFEAAI 133
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
31-193 |
6.05e-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: 6.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 31 QEARDELVEFQEGSRELEAELEA--QLVQAEQRNRDLQADNQRLKYEVEALK--------EKLEHQYAQSYKQVSVLEDD 100
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRlwfaqrrlELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 101 LSQTRAIKEQLHKYVRELEQAN--------DDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQR--- 169
Cdd:COG4913 311 LERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAeaa 390
|
170 180
....*....|....*....|....*
gi 71284108 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 |
7.38e-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: 38.19 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 21 ELSLKYKQsFQEARDEL-VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQ---------- 89
Cdd:pfam07111 478 DLSLELEQ-LREERNRLdAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQlevarqgqqe 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 90 SYKQVSVLEDDLSQTRAIKEQ-LHKYVRELE-----QANDDLERAKRA------TIVSLEDFEQRLNQAIERNAFLesel 157
Cdd:pfam07111 557 STEEAASLRQELTQQQEIYGQaLQEKVAEVEtrlreQLSDTKRRLNEArreqakAVVSLRQIQHRATQEKERNQEL---- 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 158 dekesllvsvQRLKDEARDLRQELAVReRQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENTFPSPKAIPN 237
Cdd:pfam07111 633 ----------RRLQDEARKEEGQRLAR-RVQELERDKNLMLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECS 701
|
250
....*....|....
gi 71284108 238 GFGTSPLTPSARIS 251
Cdd:pfam07111 702 ASAPIPAAVPTRES 715
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
13-173 |
9.29e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 37.84 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 13 KEEtayWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKY---EVEALKEKLEHQYAq 89
Cdd:PRK12704 63 KEE---IHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQkqqELEKKEEELEELIE- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 90 syKQVSVLED--DLSQTRAiKEQLhkyvreLEQANDDLERAKRATIvsledfeqrlnQAIERNAFLESELDEKESLLVSV 167
Cdd:PRK12704 139 --EQLQELERisGLTAEEA-KEIL------LEKVEEEARHEAAVLI-----------KEIEEEAKEEADKKAKEILAQAI 198
|
....*.
gi 71284108 168 QRLKDE 173
Cdd:PRK12704 199 QRCAAD 204
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
49-194 |
9.29e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 37.69 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 49 AELEAQLVQAEQRNRDLQADNQRLKYEVEALkeklehqyaQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERA 128
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGLVDLSEEAK---------LLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 129 KRATIVSledfeQRLNQAIERNAFLESELDEKESLLV----SVQRLKDEARDLRQELAVRERQQEVTRKS 194
Cdd:COG3206 256 LPELLQS-----PVIQQLRAQLAELEAELAELSARYTpnhpDVIALRAQIAALRAQLQQEAQRILASLEA 320
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
10-181 |
9.61e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 37.80 E-value: 9.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 10 SSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEaqlvQAEQRNRDLQADNQRLKYEVEALKEkLEHQYAQ 89
Cdd:pfam05557 107 SCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKAS----EAEQLRQNLEKQQSSLAEAEQRIKE-LEFEIQS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 90 SykqvsvlEDDLSQTRAIKEQLHKYvreleqanDDLERAKRAtivsLEDFEQRLNQAIERNAFLESELDEKESLLVSVQR 169
Cdd:pfam05557 182 Q-------EQDSEIVKNSKSELARI--------PELEKELER----LREHNKHLNENIENKLLLKEEVEDLKRKLEREEK 242
|
170
....*....|..
gi 71284108 170 LKDEARDLRQEL 181
Cdd:pfam05557 243 YREEAATLELEK 254
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
38-181 |
9.84e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 38.01 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 38 VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEhQYAQSYKQVSVLEDDLSQTRaikeqlhkyVRE 117
Cdd:COG3096 828 VAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQ-LLNKLLPQANLLADETLADR---------LEE 897
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71284108 118 LEQANDDLERAKRativSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQEL 181
Cdd:COG3096 898 LREELDAAQEAQA----FIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQI 957
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
27-149 |
9.86e-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: 36.83 E-value: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 27 KQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKE--KLEHQYAQSYKQVSVLEDDLSQT 104
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG-NVRNNKEyeALQKEIESLKRRISDLEDEILEL 115
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 71284108 105 RAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIER 149
Cdd:COG1579 116 MERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
27-193 |
9.99e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 37.57 E-value: 9.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 27 KQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRA 106
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE-QLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71284108 107 IKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRER 186
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
....*..
gi 71284108 187 QQEVTRK 193
Cdd:COG4372 189 LKEANRN 195
|
|
| |
