|
Name |
Accession |
Description |
Interval |
E-value |
| NUDE_C |
pfam04880 |
NUDE protein, C-terminal conserved region; This family represents the C-terminal conserved ... |
148-322 |
4.31e-59 |
|
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: 188.08 E-value: 4.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 148 SLEDFEQRLNQAIERNAFLESEL----DEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSSP---TLDCEKMD 220
Cdd:pfam04880 1 SLEDLESKYNQAIERGVLLEEEIkigeQERESLRIENQRLRDELSDLKQELAIRQEKLRNLLMRSPSTPslqTLEIFDRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 221 SAVQASlslpATPVG-KGTENTFPSpkAIPNGFGTSPLTPSARISAlnivgDLLRKVGALESKLAACRNFAKDQASRKSY 299
Cdd:pfam04880 81 PAVQAV----SSPVIaTPPEKSFNS--LRTGSETATPPSPPASESS-----DLLRKVGALTPKLPRCRASASDSNASRRG 149
|
170 180
....*....|....*....|...
gi 1034601562 300 isgNVNCGVLNGNGTKFSRSGHT 322
Cdd:pfam04880 150 ---NSRSLYGSRPPTKFAHSRHT 169
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
40-208 |
4.25e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 4.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 40 KQSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAqsykQVSVLEDDLSQ 116
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEEELAELEEELEELEE----ELEELEEELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 117 TRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAV 196
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
170
....*....|..
gi 1034601562 197 RERQQEVTRKSA 208
Cdd:COG1196 429 ALAELEEEEEEE 440
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
40-201 |
1.34e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 40 KQSFQEARDELVEFQEGSRELEaELEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQS-YKQVSVLEDDLS 115
Cdd:COG4913 270 RLAELEYLRAALRLWFAQRRLE-LLEAELEELRAELARLEAELERLEARLDALREEldeLEAQIRGNgGDRLEQLEREIE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 116 QTRAIKEQLhkyVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKE----SLLVSVQRLKDEARDLR 191
Cdd:COG4913 349 RLERELEER---ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEealaEAEAALRDLRRELRELE 425
|
170
....*....|
gi 1034601562 192 QELAVRERQQ 201
Cdd:COG4913 426 AEIASLERRK 435
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-208 |
1.70e-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: 56.22 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 37 LKYKQSFQEARDELVEFQEGSRELEAELEA---QLVQAEQRNRDLQADNQRLKYEVEALKEklehQYAQSYKQVSVLEDD 113
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAElrkELEELEEELEQLRKELEELSRQISALRK----DLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 114 LSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESllvSVQRLKDEARDLRQE 193
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA---ELTLLNEEAANLRER 825
|
170
....*....|....*
gi 1034601562 194 LAVRERQQEVTRKSA 208
Cdd:TIGR02168 826 LESLERRIAATERRL 840
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
26-205 |
1.79e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 26 KEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQ 102
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyeLLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 103 SYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQR 182
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180
....*....|....*....|....*...
gi 1034601562 183 LKDEARD-----LRQELAVRERQQEVTR 205
Cdd:COG1196 380 ELEELAEelleaLRAAAELAAQLEELEE 407
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
40-206 |
5.71e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.29 E-value: 5.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 40 KQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRA 119
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 120 IKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLvsvQRLKDEARDLRQELAVRER 199
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELI---EELESELEALLNERASLEE 887
|
....*..
gi 1034601562 200 QQEVTRK 206
Cdd:TIGR02168 888 ALALLRS 894
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
40-206 |
1.66e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 40 KQSFQEARDELVEFQEGSRELEaELEAQLVQAEQRNRDLQADNQRLKYEVEAL-----KEKLEHQYAQSYKQVSVLEDDL 114
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLLQLLplyqeLEALEAELAELPERLEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 115 SQTRAIKEQLHKYVRELEQANDDLERAKRATivsLEDFEQRLNQAIERNAFLESELDEKESLLvsvQRLKDEARDLRQEL 194
Cdd:COG4717 156 EELRELEEELEELEAELAELQEELEELLEQL---SLATEEELQDLAEELEELQQRLAELEEEL---EEAQEELEELEEEL 229
|
170
....*....|..
gi 1034601562 195 AVRERQQEVTRK 206
Cdd:COG4717 230 EQLENELEAAAL 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
58-205 |
1.76e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 58 RELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHqyAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDD 137
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREA--LQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 138 LERAKR---ATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDL------------RQELAVRERQQE 202
Cdd:COG4913 687 LAALEEqleELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelralleerFAAALGDAVERE 766
|
...
gi 1034601562 203 VTR 205
Cdd:COG4913 767 LRE 769
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
44-202 |
1.97e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 44 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQ 123
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA-EAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034601562 124 LhkyVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQE 202
Cdd:COG1196 412 L---LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
44-271 |
4.06e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 44 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYaQSYKQVSVLE------------ 111
Cdd:COG3883 40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY-RSGGSVSYLDvllgsesfsdfl 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 112 DDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLR 191
Cdd:COG3883 119 DRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 192 QELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENTFPSPKAIPNGFGTSPLTPSARISALNIVGD 271
Cdd:COG3883 199 AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAA 278
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
21-215 |
6.03e-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: 51.22 E-value: 6.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 21 DFSSLKEETAYWkELSLKYKqsfqEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQY 100
Cdd:TIGR02169 215 ALLKEKREYEGY-ELLKEKE----ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 101 AQSYKQVSVLEDDLSQTRAIKEQLHKYVRELE--QANDDLERakRATIVSLEDFEQRLNQAIERNAFLESELDEK----E 174
Cdd:TIGR02169 290 LRVKEKIGELEAEIASLERSIAEKERELEDAEerLAKLEAEI--DKLLAEIEELEREIEEERKRRDKLTEEYAELkeelE 367
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034601562 175 SLLVSVQRLKDEARDLRQELA-VRERQQEVTRKSAPSSPTLD 215
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDELKdYREKLEKLKREINELKRELD 409
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
23-212 |
6.15e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 23 SSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEA---ELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQ 99
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 100 YAQSYK--QVSVLE-----DDLSQT-------RAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAF 165
Cdd:COG4942 110 LRALYRlgRQPPLAlllspEDFLDAvrrlqylKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034601562 166 LESELDEKESLLVSVQR-----------LKDEARDLRQELAVRERQQEVTRKSAPSSP 212
Cdd:COG4942 190 LEALKAERQKLLARLEKelaelaaelaeLQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
41-208 |
1.26e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 41 QSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQT 117
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEElaeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 118 RAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVR 197
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
170
....*....|.
gi 1034601562 198 ERQQEVTRKSA 208
Cdd:COG1196 462 LELLAELLEEA 472
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
33-206 |
1.98e-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: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 33 KELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQaeqrnrdLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLED 112
Cdd:TIGR02168 227 LALLVLRLEELREELEELQEELKEAEEELEELTAELQE-------LEEKLEELRLEVSELEEEIEELQKELYALANEISR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 113 DLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDF---EQRLNQAIERNAFLESELDEKESLLV----SVQRLKD 185
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELaelEEKLEELKEELESLEAELEELEAELEelesRLEELEE 379
|
170 180
....*....|....*....|.
gi 1034601562 186 EARDLRQELAVRERQQEVTRK 206
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNN 400
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
52-208 |
2.17e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 52 EFQEGSRELEAELeaQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVREL 131
Cdd:COG1196 217 ELKEELKELEAEL--LLLKLRELEAELEELEAELE-ELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034601562 132 EQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSA 208
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
17-190 |
2.84e-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: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 17 EDIPDFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQ---LVQAEQRNRDLQADNQRLKYEVEALK 93
Cdd:TIGR02168 334 ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLrskVAQLELQIASLNNEIERLEARLERLE 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 94 --------EKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAF 165
Cdd:TIGR02168 414 drrerlqqEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS 493
|
170 180
....*....|....*....|....*
gi 1034601562 166 LESELDEKESLLVSVQRLKDEARDL 190
Cdd:TIGR02168 494 LERLQENLEGFSEGVKALLKNQSGL 518
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
23-208 |
7.71e-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: 47.76 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 23 SSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQ------ADNQRLKYEVEALKEKL 96
Cdd:TIGR02169 691 SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSsleqeiENVKSELKELEARIEEL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 97 EHQYAQSYKQVSVLEDDLSQTRaikeqlhkyVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESL 176
Cdd:TIGR02169 771 EEDLHKLEEALNDLEARLSHSR---------IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841
|
170 180 190
....*....|....*....|....*....|....
gi 1034601562 177 LVSVQRLKDEARDLRQEL--AVRERQQEVTRKSA 208
Cdd:TIGR02169 842 RIDLKEQIKSIEKEIENLngKKEELEEELEELEA 875
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
38-202 |
1.04e-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: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 38 KYKQSFQEARDELVEFQEGSRELEAELEA---QLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDL 114
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLE 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 115 SQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDF---EQRLNQAIERNAFLESELDEKESllvSVQRLKDEARDLR 191
Cdd:TIGR02168 845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERaslEEALALLRSELEELSEELRELES---KRSELRRELEELR 921
|
170
....*....|..
gi 1034601562 192 QELA-VRERQQE 202
Cdd:TIGR02168 922 EKLAqLELRLEG 933
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
44-209 |
1.07e-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: 46.07 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 44 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEq 123
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-DLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 124 LHKYVRELEQA---NDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKEsllvsvQRLKDEARDLRQELAVRERQ 200
Cdd:COG1579 91 YEALQKEIESLkrrISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK------AELDEELAELEAELEELEAE 164
|
....*....
gi 1034601562 201 QEVTRKSAP 209
Cdd:COG1579 165 REELAAKIP 173
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
44-195 |
2.52e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 44 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALK---EKLEHQYAQSYKQVSVLEDDLSQTRAI 120
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEeliEELESELEALLNERASLEEALALLRSE 895
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 121 KEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLV------------SVQRLKDEAR 188
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLeeaealenkiedDEEEARRRLK 975
|
....*..
gi 1034601562 189 DLRQELA 195
Cdd:TIGR02168 976 RLENKIK 982
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
43-208 |
6.43e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 43 FQEARDELVEFQE---GSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQ---YAQSYKQVSVLEDDLSQ 116
Cdd:TIGR02168 276 VSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEELKEELES 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 117 TRAIKEQLHKYVRELEQANDDLERAkrativsLEDFEQRLNQAIERNAFLESELdekESLLVSVQRLKDEARDLRQELAV 196
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQ-------LETLRSKVAQLELQIASLNNEI---ERLEARLERLEDRRERLQQEIEE 425
|
170
....*....|..
gi 1034601562 197 RERQQEVTRKSA 208
Cdd:TIGR02168 426 LLKKLEEAELKE 437
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-202 |
6.78e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 25 LKEETAYWKELSLKYKQSFQEARDELVEFqegsRELEAELEAQLVQAEQrnrdlQADNQRLKYevealkEKLEHQYAQSY 104
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEEL----EAELEELESRLEELEE-----QLETLRSKV------AQLELQIASLN 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 105 KQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVS-----LEDFEQRLNQAIERNAFLESELDEKESLLVS 179
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEeleeeLEELQEELERLEEALEELREELEEAEQALDA 479
|
170 180
....*....|....*....|...
gi 1034601562 180 vqrLKDEARDLRQELAVRERQQE 202
Cdd:TIGR02168 480 ---AERELAQLQARLDSLERLQE 499
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
35-162 |
8.43e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 35 LSLKyKQSFQEARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKekleHQYAQSYKQVSVLE 111
Cdd:PRK09039 69 LSLE-RQGNQDLQDSVANLRASLSAAEAErsrLQALLAELAGAGAAAEGRAGELAQELDSEK----QVSARALAQVELLN 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1034601562 112 DDLSqtrAIKEQLHKyvreLEQANDDLERAKRATIVSLEDFEQRLNQAIER 162
Cdd:PRK09039 144 QQIA---ALRRQLAA----LEAALDASEKRDRESQAKIADLGRRLNVALAQ 187
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
40-205 |
9.12e-05 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 9.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 40 KQSFQEARDEL----VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKE-----KLEHQYA-QSYKQV-- 107
Cdd:pfam12128 645 RTALKNARLDLrrlfDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEeqkeqKREARTEkQAYWQVve 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 108 ---SVLEDDLSQTRAIKEQLHK---------YVREL------EQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESE 169
Cdd:pfam12128 725 galDAQLALLKAAIAARRSGAKaelkaletwYKRDLaslgvdPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQET 804
|
170 180 190
....*....|....*....|....*....|....*..
gi 1034601562 170 -LDEKESLLVSVQRLKDEARDLRQELAvreRQQEVTR 205
Cdd:pfam12128 805 wLQRRPRLATQLSNIERAISELQQQLA---RLIADTK 838
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
63-205 |
9.48e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 9.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 63 ELEAQLVQAEQRNRDLQADNQRLKY---EVEALKEKLEH--QYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQAndd 137
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEEleeELEELEAELEElrEELEKLEKLLQLLPLYQELEALEAELAELPERLEEL--- 151
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 138 leRAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLV--SVQRLKDEARDLRQELAVRERQQEVTR 205
Cdd:COG4717 152 --EERLEELRELEEELEELEAELAELQEELEELLEQLSLATeeELQDLAEELEELQQRLAELEEELEEAQ 219
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
25-238 |
1.00e-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: 44.29 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 25 LKEETAYWKElslkYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALK----------E 94
Cdd:TIGR02169 838 LQEQRIDLKE----QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELErkieeleaqiE 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 95 KLEHQYAQSYKQVSVLEDDLSQTRAIK-------------EQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIE 161
Cdd:TIGR02169 914 KKRKRLSELKAKLEALEEELSEIEDPKgedeeipeeelslEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKE 993
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034601562 162 RNAFLESELDEKESLLVSVQRLKDEARdLRQELAVRERQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGT 238
Cdd:TIGR02169 994 KRAKLEEERKAILERIEEYEKKKREVF-MEAFEAINENFNEIFAELSGGTGELILENPDDPFAGGLELSAKPKGKPV 1069
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
40-196 |
1.04e-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: 44.17 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 40 KQSFQEARDELVEFQEGSRELEAELEA-----QLVQAEQRnrdLQADNQRLKYEVEALKEKLEHQ---YAQSYKQVSVLE 111
Cdd:COG3096 305 QYRLVEMARELEELSARESDLEQDYQAasdhlNLVQTALR---QQEKIERYQEDLEELTERLEEQeevVEEAAEQLAEAE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 112 DDLSQTRA----IKEQLHKYVRELE----------QANDDLERAKR---ATIVSLEDFEQRLnqaiernafleSELDEKE 174
Cdd:COG3096 382 ARLEAAEEevdsLKSQLADYQQALDvqqtraiqyqQAVQALEKARAlcgLPDLTPENAEDYL-----------AAFRAKE 450
|
170 180
....*....|....*....|..
gi 1034601562 175 sllvsvQRLKDEARDLRQELAV 196
Cdd:COG3096 451 ------QQATEEVLELEQKLSV 466
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
37-209 |
1.93e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 37 LKYKQSFQEARDELVEFQEGSRELE---AELEAQLV----QAE--QRNRDLQADNQRLK-----YEVEALKEKLEH---Q 99
Cdd:TIGR02168 168 SKYKERRKETERKLERTRENLDRLEdilNELERQLKslerQAEkaERYKELKAELRELElallvLRLEELREELEElqeE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 100 YAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVS 179
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190
....*....|....*....|....*....|
gi 1034601562 180 VQRLKDEARDLRQELAVRERQQEVTRKSAP 209
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKEELESLE 357
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
38-211 |
3.87e-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: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 38 KYKQSFQEARDELVEFQEGSRELEAELEA-----QLVQAEQRNRDLQADNQRLKYEVEALKEKLEH-------------- 98
Cdd:COG3206 186 ELRKELEEAEAALEEFRQKNGLVDLSEEAklllqQLSELESQLAEARAELAEAEARLAALRAQLGSgpdalpellqspvi 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 99 -QYAQSYKQVSVLEDDLSQT--------RAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESE 169
Cdd:COG3206 266 qQLRAQLAELEAELAELSARytpnhpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE 345
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034601562 170 LDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAPSS 211
Cdd:COG3206 346 LPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
51-200 |
5.50e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 51 VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALK--EKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYV 128
Cdd:PRK02224 467 VETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDriERLEERREDLEELIAERRETIEEKRERAEELRERA 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 129 RELE--------QANDDLERA--KRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLkdeaRDLRQELAVRE 198
Cdd:PRK02224 547 AELEaeaeekreAAAEAEEEAeeAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERL----REKREALAELN 622
|
..
gi 1034601562 199 RQ 200
Cdd:PRK02224 623 DE 624
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
33-206 |
7.34e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 33 KELSLKYKQSFQEARDELVEFQEGSRELEAEL---------EAQLVQAEQRNRDLQADNQRLK-YEVEALK------EKL 96
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELrelekvlkkESELIKLKELAEQLKELEEKLKkYNLEELEkkaeeyEKL 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 97 EHQYAQSYKQVSVLEDDL-------SQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESE 169
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELekleelkKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDA 610
|
170 180 190
....*....|....*....|....*....|....*..
gi 1034601562 170 LDEKESLLVSVQRLKDEARDLRQELAVRERQQEVTRK 206
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETEKRLEELRK 647
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
25-203 |
7.40e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 7.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 25 LKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQlvqaeQRNRDLQADNQRLKYEVEALKEKLEH------ 98
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESL-----ERIRTLLAAIADAEDEIERLREKREAlaelnd 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 99 ----QYAQSYKQVSVLEDD-----LSQTRAIKEQLHKYVRELEQANDDLERAK---RATIVSLEDFEQRLNQAIERNAFL 166
Cdd:PRK02224 624 erreRLAEKRERKRELEAEfdearIEEAREDKERAEEYLEQVEEKLDELREERddlQAEIGAVENELEELEELRERREAL 703
|
170 180 190
....*....|....*....|....*....|....*..
gi 1034601562 167 ESELDEKESLLVSVQRLKDEARDLRQELavreRQQEV 203
Cdd:PRK02224 704 ENRVEALEALYDEAEELESMYGDLRAEL----RQRNV 736
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
45-193 |
7.66e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 45 EARDELV---EFQEGSRE----LEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQSYKQVSVLEDDL 114
Cdd:PRK02224 293 EERDDLLaeaGLDDADAEaveaRREELEDRDEELRDRLEECRVAAQAHNEEAESLREDaddLEERAEELREEAAELESEL 372
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034601562 115 SQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQE 193
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
48-202 |
8.02e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 48 DELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQrlkyevealkeklehQYAQSYKQVSVLEDDLSQTRAIK------ 121
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHS---------------QFEQAYQLVRKIAGEVSRSEAWDvarell 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 122 -------------EQLHKYVRELEQANDDLERAKRAtivsLEDFEQRLNQAIERNAFLESELDEKESLLVSvqrLKDEAR 188
Cdd:PRK04863 503 rrlreqrhlaeqlQQLRMRLSELEQRLRQQQRAERL----LAEFCKRLGKNLDDEDELEQLQEELEARLES---LSESVS 575
|
170
....*....|....
gi 1034601562 189 DLRQELAVRERQQE 202
Cdd:PRK04863 576 EARERRMALRQQLE 589
|
|
| PRK13922 |
PRK13922 |
rod shape-determining protein MreC; Provisional |
156-202 |
9.36e-04 |
|
rod shape-determining protein MreC; Provisional
Pssm-ID: 237560 Cd Length: 276 Bit Score: 40.35 E-value: 9.36e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1034601562 156 LNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQE 202
Cdd:PRK13922 71 LFDLREENEELKKELLELESRLQELEQLEAENARLRELLNLKESLDY 117
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
54-207 |
9.69e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 54 QEGSRELEAELEaQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRA----IKEQLHKYVR 129
Cdd:COG4942 19 ADAAAEAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAelaeLEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 130 ELEQANDDLERAKRAT-----------IVSLEDFEQ--RLNQAIER-NAFLESELDEKESLLVSVQRLKDEARDLRQELA 195
Cdd:COG4942 98 ELEAQKEELAELLRALyrlgrqpplalLLSPEDFLDavRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170
....*....|..
gi 1034601562 196 VRERQQEVTRKS 207
Cdd:COG4942 178 ALLAELEEERAA 189
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
44-195 |
1.07e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 44 QEARDELVEFQEGSRELEA------ELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQ--------SYKQVSV 109
Cdd:COG4913 671 AELEAELERLDASSDDLAAleeqleELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaedlaRLELRAL 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 110 LEDDLSQ----------TRAIKEQLHKYVRELEQANDDLERAKR--------------ATIVSLEDFEQRLNQAIE---- 161
Cdd:COG4913 751 LEERFAAalgdaverelRENLEERIDALRARLNRAEEELERAMRafnrewpaetadldADLESLPEYLALLDRLEEdglp 830
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1034601562 162 ------RNAFLESELDEKESLLvsvQRLKDEARDLRQELA 195
Cdd:COG4913 831 eyeerfKELLNENSIEFVADLL---SKLRRAIREIKERID 867
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
45-225 |
1.18e-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: 40.82 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 45 EARDELVEFQEGSRELEAE---LEAQLVQAEQRNRDLQADNQRLKYEVEALKEK---LEHQYAQSYKQVSVLEDDLSQTR 118
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEEvsrIEARLREIEQKLNRLTLEKEYLEKEIQELQEQridLKEQIKSIEKEIENLNGKKEELE 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 119 AIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQaiernafLESELDEKESLLvsvQRLKDEARDLRQELAVRE 198
Cdd:TIGR02169 868 EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE-------LEAQIEKKRKRL---SELKAKLEALEEELSEIE 937
|
170 180
....*....|....*....|....*..
gi 1034601562 199 RqqEVTRKSAPSSPTLDCEKMDSAVQA 225
Cdd:TIGR02169 938 D--PKGEDEEIPEEELSLEDVQAELQR 962
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
44-161 |
1.21e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.58 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 44 QEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQAdnqrLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQT--RAIK 121
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEA----LLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqQAIK 580
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1034601562 122 E------QLHKYVRELEQANDDLERAKRativsLEDFEQRLNQAIE 161
Cdd:PRK00409 581 EakkeadEIIKELRQLQKGGYASVKAHE-----LIEARKRLNKANE 621
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
62-203 |
1.26e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.03 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 62 AELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKlehqyaqsykqvsvleddlsqtRAIKEQLHKYVRELEQANDDLERA 141
Cdd:COG1566 79 TDLQAALAQAEAQLAAAEAQLARLEAELGAEAEI----------------------AAAEAQLAAAQAQLDLAQRELERY 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034601562 142 KRAT---IVSLEDFEQRLNQAIErnafLESELDEKESLLVSVQRLKDEARDLRQ-ELAVRERQQEV 203
Cdd:COG1566 137 QALYkkgAVSQQELDEARAALDA----AQAQLEAAQAQLAQAQAGLREEEELAAaQAQVAQAEAAL 198
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
54-209 |
1.29e-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: 40.71 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 54 QEGSRELEAELEAQLVQAEQRNRDLQadnQRLkyeveALKEKLEHQYAQSYKQVSVLEDDLSQTRA---IKEQLHKY--- 127
Cdd:COG3096 436 PENAEDYLAAFRAKEQQATEEVLELE---QKL-----SVADAARRQFEKAYELVCKIAGEVERSQAwqtARELLRRYrsq 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 128 -------------VRELEQANDDLERAKRativSLEDFEQRLNQAIERNAFLESELDE----KESLLVSVQRLKDEARDL 190
Cdd:COG3096 508 qalaqrlqqlraqLAELEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAEleaqLEELEEQAAEAVEQRSEL 583
|
170 180
....*....|....*....|
gi 1034601562 191 RQEL-AVRERQQEVTRKsAP 209
Cdd:COG3096 584 RQQLeQLRARIKELAAR-AP 602
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
38-202 |
1.92e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.08 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 38 KYKQSFQEARDELVEFQEGSREL--EAELEAQLVQAEQRNRDLQADNQRlkyevealKEKLEHQYAQSYKQvsvleddls 115
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKleAALLEAKELLLRERNQQRQEARRE--------REELQREEERLVQK--------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 116 qtraiKEQLHKYVRELEQANDDLERAKRAtivsledFEQRLNQAIERNAFLESELDEKESLLVSVQR---LKDEARDLRQ 192
Cdd:PRK12705 90 -----EEQLDARAEKLDNLENQLEEREKA-------LSARELELEELEKQLDNELYRVAGLTPEQARkllLKLLDAELEE 157
|
170
....*....|
gi 1034601562 193 ELAVRERQQE 202
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 ... |
57-213 |
2.09e-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: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 57 SRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYkqvsvleddlSQTRAIKEQLHKYVRELEQAND 136
Cdd:pfam00529 56 YQAALDSAEAQLAKAQAQVARLQAELDRLQ-ALESELAISRQDYDGAT----------AQLRAAQAAVKAAQAQLAQAQI 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 137 DLERAK-RATI--VSLEDF-EQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELA-----VRERQQEVTRKS 207
Cdd:pfam00529 125 DLARRRvLAPIggISRESLvTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSgaqlqIAEAEAELKLAK 204
|
....*.
gi 1034601562 208 APSSPT 213
Cdd:pfam00529 205 LDLERT 210
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
25-196 |
2.14e-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: 40.09 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 25 LKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSY 104
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 105 KQVSVLeddLSQTRAIKEQLHKYVRELEQANDDLERAKRATIVSLEDfeqrLNQAIERNAFLESELdekESLLVSVQRLK 184
Cdd:pfam05483 240 KQVSLL---LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDEN----LKELIEKKDHLTKEL---EDIKMSLQRSM 309
|
170
....*....|..
gi 1034601562 185 DEARDLRQELAV 196
Cdd:pfam05483 310 STQKALEEDLQI 321
|
|
| FtsB |
COG2919 |
Cell division protein FtsB [Cell cycle control, cell division, chromosome partitioning]; |
62-97 |
2.23e-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: 2.23e-03
10 20 30
....*....|....*....|....*....|....*.
gi 1034601562 62 AELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLE 97
Cdd:COG2919 32 RELRQEIAELEAENAKLKARNAELEAEVADLKDGPD 67
|
|
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
42-167 |
2.25e-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: 39.29 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 42 SFQEARDELVEFQEGSREleaeleAQLVQAeqrnrdlQADNQR--LKYEVEALKEKLEHqyaqsykqvsvLEDDLSQTRa 119
Cdd:pfam09738 87 SLRDIKHELKEVEEKYRK------AMISNA-------QLDNEKsnLMYQVDLLKDKLEE-----------MEESLAELQ- 141
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1034601562 120 ikeqlhkyvRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLE 167
Cdd:pfam09738 142 ---------RELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIE 180
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
25-224 |
2.32e-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: 39.95 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 25 LKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELE-----AELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQ 99
Cdd:TIGR00618 251 AQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaAPLAAHIKAVTQIEQQAQRIHTELQ-SKMRSRAKLLMK 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 100 YAQSYKQvsvlEDDLSQTRAIKEQLHKYVRELEQANDD----LERAKRATIVS--LEDFEQRLNQAIERNAFLESELDEK 173
Cdd:TIGR00618 330 RAAHVKQ----QSSIEEQRRLLQTLHSQEIHIRDAHEVatsiREISCQQHTLTqhIHTLQQQKTTLTQKLQSLCKELDIL 405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034601562 174 ESLLVSVQRLKDEARDLRQELAVRERQQEVTRKSAP-----SSPTLDCEKMDSAVQ 224
Cdd:TIGR00618 406 QREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAElcaaaITCTAQCEKLEKIHL 461
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
54-208 |
2.97e-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: 39.11 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 54 QEGSRELEAELEAQLVQAEQRNRDlqadnqrlKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQLHKYVRELEQ 133
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKE--------KERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034601562 134 ANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLvsvQRLKDeardlRQELAVRERQQEVTRKSA 208
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETEL---ERMKE-----RAKKAGAQRKEEEAERKQ 175
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
34-264 |
3.07e-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: 39.35 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 34 ELSLKYKQsFQEARDEL-VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQ---------- 102
Cdd:pfam07111 478 DLSLELEQ-LREERNRLdAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQlevarqgqqe 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 103 SYKQVSVLEDDLSQTRAIKEQ-LHKYVRELE-----QANDDLERAKRA------TIVSLEDFEQRLNQAIERNAFLesel 170
Cdd:pfam07111 557 STEEAASLRQELTQQQEIYGQaLQEKVAEVEtrlreQLSDTKRRLNEArreqakAVVSLRQIQHRATQEKERNQEL---- 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 171 dekesllvsvQRLKDEARDLRQELAVReRQQEVTRKSAPSSPTLDCEKMDSAVQASLSLPATPVGKGTENTFPSPKAIPN 250
Cdd:pfam07111 633 ----------RRLQDEARKEEGQRLAR-RVQELERDKNLMLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECS 701
|
250
....*....|....
gi 1034601562 251 GFGTSPLTPSARIS 264
Cdd:pfam07111 702 ASAPIPAAVPTRES 715
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
19-197 |
3.97e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 19 IPDFSSLKEETaywkelslkYKQSFQEARDELVEFQEGSR----------ELEAEL------EAQLVQAEQRNRDLQADN 82
Cdd:PRK04863 881 LPRLNLLADET---------LADRVEEIREQLDEAEEAKRfvqqhgnalaQLEPIVsvlqsdPEQFEQLKQDYQQAQQTQ 951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 83 QRLKYEVEALKEKLEHQYAQSYKQVsvlEDDLSQTRAIKEQLHkyvRELEQANDDLERAKRAtivsLEDFEQRLNQAIER 162
Cdd:PRK04863 952 RDAKQQAFALTEVVQRRAHFSYEDA---AEMLAKNSDLNEKLR---QRLEQAEQERTRAREQ----LRQAQAQLAQYNQV 1021
|
170 180 190
....*....|....*....|....*....|....*
gi 1034601562 163 NAFLESELDEKEsllvsvQRLKDEARDLrQELAVR 197
Cdd:PRK04863 1022 LASLKSSYDAKR------QMLQELKQEL-QDLGVP 1049
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
58-160 |
4.29e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 37.96 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 58 RELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQyaQSYKQvsvledDLSQTRAIKEQLHKYVRELEQANDD 137
Cdd:pfam13851 39 KKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENY--EKDKQ------SLKNLKARLKVLEKELKDLKWEHEV 110
|
90 100
....*....|....*....|...
gi 1034601562 138 LERAKRATIVSLEDFEQRLNQAI 160
Cdd:pfam13851 111 LEQRFEKVERERDELYDKFEAAI 133
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
40-206 |
5.29e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.34 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 40 KQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRA 119
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE-QLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 120 IKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRER 199
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
....*..
gi 1034601562 200 QQEVTRK 206
Cdd:COG4372 189 LKEANRN 195
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
44-206 |
5.30e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 38.74 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 44 QEARDELVEFQEGSRELEAELEA--QLVQAEQRNRDLQADNQRLKYEVEALK--------EKLEHQYAQSYKQVSVLEDD 113
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELlePIRELAERYAAARERLAELEYLRAALRlwfaqrrlELLEAELEELRAELARLEAE 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 114 LSQTRAIKEQLHKYVRELEQAN--------DDLERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQR--- 182
Cdd:COG4913 311 LERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAeaa 390
|
170 180
....*....|....*....|....*
gi 1034601562 183 -LKDEARDLRQELAVRERQQEVTRK 206
Cdd:COG4913 391 aLLEALEEELEALEEALAEAEAALR 415
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
23-194 |
5.97e-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: 38.57 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 23 SSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELEAELEaqlvQAEQRNRDLQADNQRLKYEVEALKEkLEHQYAQ 102
Cdd:pfam05557 107 SCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKAS----EAEQLRQNLEKQQSSLAEAEQRIKE-LEFEIQS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 103 SykqvsvlEDDLSQTRAIKEQLHKYvreleqanDDLERAKRAtivsLEDFEQRLNQAIERNAFLESELDEKESLLVSVQR 182
Cdd:pfam05557 182 Q-------EQDSEIVKNSKSELARI--------PELEKELER----LREHNKHLNENIENKLLLKEEVEDLKRKLEREEK 242
|
170
....*....|..
gi 1034601562 183 LKDEARDLRQEL 194
Cdd:pfam05557 243 YREEAATLELEK 254
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
62-209 |
6.31e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 37.24 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 62 AELEAQLVQAEQR-----NRDLQADNQRLKYEVEALKEKLEhQYAQSYKQvsVLEDDLSQTRAikeQLHKYVREL-EQAN 135
Cdd:pfam01442 14 EELQEQLGPVAQElvdrlEKETEALRERLQKDLEEVRAKLE-PYLEELQA--KLGQNVEELRQ---RLEPYTEELrKRLN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034601562 136 DDLERAKRATIVSLEDFEQRLNQAIER-NAFLESELDE-KESLLVSVQRLKDEARDLRQEL--AVRERQQEVTRKSAP 209
Cdd:pfam01442 88 ADAEELQEKLAPYGEELRERLEQNVDAlRARLAPYAEElRQKLAERLEELKESLAPYAEEVqaQLSQRLQELREKLEP 165
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
40-162 |
6.76e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 37.60 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 40 KQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKyEVEALKE--KLEHQYAQSYKQVSVLEDDLSQT 117
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG-NVRNNKEyeALQKEIESLKRRISDLEDEILEL 115
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1034601562 118 RAIKEQLHKYVRELEQANDDLERAKRATIVSLEDFEQRLNQAIER 162
Cdd:COG1579 116 MERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
26-186 |
7.62e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 37.84 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 26 KEEtayWKELSLKYKQSFQEARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKY---EVEALKEKLEHQYAq 102
Cdd:PRK12704 63 KEE---IHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQkqqELEKKEEELEELIE- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 103 syKQVSVLED--DLSQTRAiKEQLhkyvreLEQANDDLERAKRATIvsledfeqrlnQAIERNAFLESELDEKESLLVSV 180
Cdd:PRK12704 139 --EQLQELERisGLTAEEA-KEIL------LEKVEEEARHEAAVLI-----------KEIEEEAKEEADKKAKEILAQAI 198
|
....*.
gi 1034601562 181 QRLKDE 186
Cdd:PRK12704 199 QRCAAD 204
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
51-194 |
8.40e-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: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 51 VEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEhQYAQSYKQVSVLEDDLSQTRaikeqlhkyVRE 130
Cdd:COG3096 828 VAFAPDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQ-LLNKLLPQANLLADETLADR---------LEE 897
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034601562 131 LEQANDDLERAKRativSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQEL 194
Cdd:COG3096 898 LREELDAAQEAQA----FIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQI 957
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
26-203 |
8.75e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 38.01 E-value: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 26 KEETAYWKELSLKYKQSFQEARdELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEklEHQYAQSYK 105
Cdd:COG5185 301 YTKSIDIKKATESLEEQLAAAE-AEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVG--EVELSKSSE 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 106 QvsvLEDDLSQTRAIKEQLHKYVRELEQANDD----LERAKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQ 181
Cdd:COG5185 378 E---LDSFKDTIESTKESLDEIPQNQRGYAQEilatLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVM 454
|
170 180
....*....|....*....|..
gi 1034601562 182 RLKDEARDLRQELAVRERQQEV 203
Cdd:COG5185 455 READEESQSRLEEAYDEINRSV 476
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
41-192 |
8.82e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 38.01 E-value: 8.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 41 QSFQEARDELVEFqEGSRELEAELEAQLVQAEQR-NRDLQ--ADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQT 117
Cdd:PRK04863 513 EQLQQLRMRLSEL-EQRLRQQQRAERLLAEFCKRlGKNLDdeDELEQLQEELEARLESLSESVSEARERRMALRQQLEQL 591
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034601562 118 RAIKEQLHKYVRELEQANDDLERAKRATIVSLEDfEQRLNQAIERNAFLESELDEKESLLVS-VQRLKDEARDLRQ 192
Cdd:PRK04863 592 QARIQRLAARAPAWLAAQDALARLREQSGEEFED-SQDVTEYMQQLLERERELTVERDELAArKQALDEEIERLSQ 666
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
45-208 |
9.71e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 38.03 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 45 EARDELVEFQEGSRELEAELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLEHQYAQSYKQVSVLEDDLSQTRAIKEQL 124
Cdd:pfam02463 153 ERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 125 hKYVRELEQANDDLERAKRATIVSledfEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERQQEVT 204
Cdd:pfam02463 233 -KLNEERIDLLQELLRDEQEEIES----SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
....
gi 1034601562 205 RKSA 208
Cdd:pfam02463 308 RKVD 311
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
21-142 |
9.81e-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: 37.74 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 21 DFSSLKEETAYWKELSLKYKQSFQEARDELVEFQEGSRELE---AELEAQLVQAEQRNRDLQADNQRLKYEVEALKEKLE 97
Cdd:TIGR02169 379 EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSeelADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLE 458
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1034601562 98 HQYAQsykqvsvLEDDLSQTRAIKEQLHKYVRELEQANDDLERAK 142
Cdd:TIGR02169 459 QLAAD-------LSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
41-205 |
9.90e-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: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 41 QSFQEARDELVEF--QEGSRELEAELEAQLVQAEQRNRDLQadnqrlkyEVEALKEKLEHQYAQSYKQVSVLEDDLSQTR 118
Cdd:COG3096 492 QAWQTARELLRRYrsQQALAQRLQQLRAQLAELEQRLRQQQ--------NAERLLEEFCQRIGQQLDAAEELEELLAELE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034601562 119 AIKEQLHKYVRELEQANDDLER---AKRATIVSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQrlkdearDLRQELA 195
Cdd:COG3096 564 AQLEELEEQAAEAVEQRSELRQqleQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVT-------AAMQQLL 636
|
170
....*....|
gi 1034601562 196 VRERQQEVTR 205
Cdd:COG3096 637 EREREATVER 646
|
|
| |
