|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
1-268 |
3.02e-117 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 341.90 E-value: 3.02e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 1 QNLEPLFEQYINNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAK 80
Cdd:pfam00038 46 SRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 81 ADTLTDEINFLRALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTA 160
Cdd:pfam00038 126 IESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 161 GRHGDDLRNTKQEIAEINRMIQRLRSESDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKE 240
Cdd:pfam00038 206 ARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLRE 285
|
250 260
....*....|....*....|....*...
gi 34069 241 YQELMNVKLALDVEIATYRKLLEGEECR 268
Cdd:pfam00038 286 YQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-250 |
6.67e-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: 48.13 E-value: 6.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 7 FEQYINNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTD 86
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 87 EINFLRAlydaELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQ---RSRAEAESWYQtKYEELQVTAGRH 163
Cdd:TIGR02168 818 EAANLRE----RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEElieELESELEALLN-ERASLEEALALL 892
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 164 GDDLRNTKQEIAEINRMIQRLRSESDHVKKQCANLQAAIADAEQR-----------GEMALKDAKNKLEGLEDALQKAKQ 232
Cdd:TIGR02168 893 RSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRidnlqerlseeYSLTLEEAEALENKIEDDEEEARR 972
|
250
....*....|....*...
gi 34069 233 DLARLLKEYQELMNVKLA 250
Cdd:TIGR02168 973 RLKRLENKIKELGPVNLA 990
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
96-236 |
7.38e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 47.27 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 96 DAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEiAQRSRAEAESWYQTKYEELQVTAGRHGD---DLRNTKQ 172
Cdd:PRK09039 52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34069 173 EIAEINRMIQRLRSESDHVKKQCANLQAAIADAEQRGemalKDAKNKLEG----LEDALQKAKQDLAR 236
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADlgrrLNVALAQRVQELNR 194
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
11-244 |
3.53e-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: 45.83 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 11 INNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYE------DEINKRTAA--ENEFVTLKKDVDAAYMNKVELQAKAD 82
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEeieqllEELNKKIKDlgEEEQLRVKEKIGELEAEIASLERSIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 83 TLTDEINFL---RALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVT 159
Cdd:TIGR02169 312 EKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 160 agrhgDDLRNTKQEIAEINRMIQRLRSESDHVKKQCANLQAAIADAEQR----------GEMALKDAKNKLEGLEDALQK 229
Cdd:TIGR02169 392 -----EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineleeekedKALEIKKQEWKLEQLAADLSK 466
|
250
....*....|....*
gi 34069 230 AKQDLARLLKEYQEL 244
Cdd:TIGR02169 467 YEQELYDLKEEYDRV 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
14-263 |
5.85e-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: 45.06 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 14 LRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRA 93
Cdd:TIGR02169 679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 94 L---YDAELSQMQTHISdtSVVLSMDNNRNLDLDSIIAEVKAQYEEI-AQRSRAEAeswyqtKYEELQVTAGRHGDDLRN 169
Cdd:TIGR02169 759 ElkeLEARIEELEEDLH--KLEEALNDLEARLSHSRIPEIQAELSKLeEEVSRIEA------RLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 170 TKQEIAEINRMIQRLRSESDHVKKQCANLQAAIADAEQRgemaLKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKL 249
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE----LEELEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
250
....*....|....
gi 34069 250 ALDVEIATYRKLLE 263
Cdd:TIGR02169 907 ELEAQIEKKRKRLS 920
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
123-272 |
1.02e-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: 44.28 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 123 LDSIIAEVKAQYEEIAQRSRAEAESWYQTKYE--ELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSESDHVKKQCANLQA 200
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEvsELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34069 201 AIADAEQRGEMA---LKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRK---LLEGEECRLNGE 272
Cdd:TIGR02168 324 QLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNE 401
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-272 |
1.61e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 27 RLDSELRGMQDlvEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHI 106
Cdd:COG1196 224 ELEAELLLLKL--RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 107 SDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESwyQTKYEELQvtagrhgDDLRNTKQEIAEINRMIQRLRS 186
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEEL--EEELEEAE-------EELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 187 ESDHVKKQcanlQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEE 266
Cdd:COG1196 373 ELAEAEEE----LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAA 448
|
....*.
gi 34069 267 CRLNGE 272
Cdd:COG1196 449 EEEAEL 454
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
24-270 |
2.16e-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: 43.12 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 24 ERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDAELSQMQ 103
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 104 THISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRA-----EAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEIN 178
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEElkalrEALDELRAELTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 179 RMIQRLRSESDHVKKQCANLQAAIADAEQRGEMALKDAKNKLE----------GLEDALQKAKQDLARLLKEYQELMNVK 248
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNerasleealaLLRSELEELSEELRELESKRSELRREL 917
|
250 260
....*....|....*....|..
gi 34069 249 LALDVEIATYRKLLEGEECRLN 270
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRID 939
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
8-263 |
3.07e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 8 EQYIN-NLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDeinkrTAAENEFVTLKKDVDAAYMNKVELQAKADTLTD 86
Cdd:COG3206 159 EAYLEqNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 87 EINFLRALYDAELSQMQTHISDTSVVLSmdnnrnldlDSIIAEVKAQYEEIaqrsraeaeswyQTKYEELQVTAGRHGDD 166
Cdd:COG3206 234 ELAEAEARLAALRAQLGSGPDALPELLQ---------SPVIQQLRAQLAEL------------EAELAELSARYTPNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 167 LRNTKQEIAEINRMIQRLrsesdhVKKQCANLQAAIADAEQRgemalkdaknkLEGLEDALQKAKQDLARLLKEYQELMN 246
Cdd:COG3206 293 VIALRAQIAALRAQLQQE------AQRILASLEAELEALQAR-----------EASLQAQLAQLEARLAELPELEAELRR 355
|
250
....*....|....*..
gi 34069 247 VKLALDVEIATYRKLLE 263
Cdd:COG3206 356 LEREVEVARELYESLLQ 372
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
122-260 |
3.14e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 122 DLDSIIAEVKAQYEEIAQRSRAEAEswyqtKYEELQVT-AGRHGDDLRNTKQEIAEINRMIQRLRSESDHVKKQCANLQA 200
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALRE-----ELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGL 373
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 201 AIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRK 260
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
166-247 |
4.21e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 166 DLRNTKQEIAEINRMIQRLRSESDHVKKQCANLQAAIADAEQR---GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQ 242
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
....*
gi 34069 243 ELMNV 247
Cdd:COG4942 108 ELLRA 112
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
11-244 |
4.30e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 11 INNLRRQLDSIVGERGRLDsELRGMQDLVEDFKnkYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINF 90
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAE-RYQALLKEKREYE--GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 91 LRALydaeLSQMQTHISDtsvvlsMDNNRNLDLDSIIAEVKAqyeEIAQRSRAEAEswYQTKYEELQVTAGRHGDDLRNT 170
Cdd:TIGR02169 270 IEQL----LEELNKKIKD------LGEEEQLRVKEKIGELEA---EIASLERSIAE--KERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 171 KQEIAEINRMIQRLRSESDHVKKQCANLQAAIADAEQRGE----------MALKDAKNKLEGLEDALQKAKQDLARLLKE 240
Cdd:TIGR02169 335 LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEevdkefaetrDELKDYREKLEKLKREINELKRELDRLQEE 414
|
....
gi 34069 241 YQEL 244
Cdd:TIGR02169 415 LQRL 418
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
17-244 |
6.25e-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: 41.97 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 17 QLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFL---RA 93
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 94 LYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRA------EAESWYQ---TKYEELQVTAGRHG 164
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESleaeleELEAELEeleSRLEELEEQLETLR 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 165 DDLRNTKQEIAEINRMIQRLRSESDHVKKQCANLQAAIADAEQR-GEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQE 243
Cdd:TIGR02168 386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEE 465
|
.
gi 34069 244 L 244
Cdd:TIGR02168 466 L 466
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-266 |
9.32e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 1 QNLEPLFEQyINNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEdEINKRTAAENEfvtLKKDVDaAYMNKVELQAK 80
Cdd:PRK03918 231 KELEELKEE-IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIE-ELEEKVKELKE---LKEKAE-EYIKLSEFYEE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 81 ADTLTDEINFLRALYDAELSQMQTHISDtsvvLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAeaeswyqtkYEELQVTA 160
Cdd:PRK03918 305 YLDELREIEKRLSRLEEEINGIEERIKE----LEEKEERLEELKKKLKELEKRLEELEERHEL---------YEEAKAKK 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 161 GR-HGDDLRNTKQEIAEINRMIQRLRSESDHVKKQCANLQAAIADAEQRGE------MALKDAKNKL---------EGLE 224
Cdd:PRK03918 372 EElERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKelkkaiEELKKAKGKCpvcgrelteEHRK 451
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 34069 225 DALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEE 266
Cdd:PRK03918 452 ELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
165-244 |
9.84e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 9.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 165 DDLRNTKQEIAEINRMIQRLRSESDHVKKQCANLQAAIADAEQRgemaLKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 244
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
56-260 |
1.48e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 56 AENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYD---AELSQMQTHISDTsvvlsmdnnrNLDLDSIIAEVKA 132
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNelqAELEALQAEIDKL----------QAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 133 QYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRN---TKQEIAEINRMIQRLRSEsdhvKKQCANLQAAIADAEQRG 209
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVLLGSESFSDFLDRlsaLSKIADADADLLEELKAD----KAELEAKKAELEAKLAEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 34069 210 EMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRK 260
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
12-237 |
1.81e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.16 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 12 NNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFL 91
Cdd:pfam01576 499 NSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRL 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 92 RalydAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVK---AQYEEiaQRSRAEAESwyqTKYEELQVTAGRHGDDLR 168
Cdd:pfam01576 579 Q----QELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKaisARYAE--ERDRAEAEA---REKETRALSLARALEEAL 649
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34069 169 NTKQEIAEINRMIQ----RLRSESDHVKKQCANLQAAIADAEQrgemALKDAKNKLEGLEDALQKAKQDLARL 237
Cdd:pfam01576 650 EAKEELERTNKQLRaemeDLVSSKDDVGKNVHELERSKRALEQ----QVEEMKTQLEELEDELQATEDAKLRL 718
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
23-246 |
3.26e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 23 GERGRLDSELRGMQDLVEDFKNkyedeINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRAL-----YDA 97
Cdd:COG4913 587 GTRHEKDDRRRIRSRYVLGFDN-----RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLaeyswDEI 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 98 ELSQMQTHISDTSVVLsmdnnRNLDLDS-IIAEVKAQYEEiAQRSRAEAESwyqtKYEELQVTAGRHgddlrntKQEIAE 176
Cdd:COG4913 662 DVASAEREIAELEAEL-----ERLDASSdDLAALEEQLEE-LEAELEELEE----ELDELKGEIGRL-------EKELEQ 724
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 177 INRMIQRLRSESDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMN 246
Cdd:COG4913 725 AEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMR 794
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
165-271 |
4.15e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 165 DDLRNTKQEIAEINRMIQRLRSESDHVKKQCANL----------------QAAIADAEQRGEmALKDAKNKLEGLEDALQ 228
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALqrlaeyswdeidvasaEREIAELEAELE-RLDASSDDLAALEEQLE 695
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 34069 229 KAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNG 271
Cdd:COG4913 696 ELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA 738
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
24-244 |
4.91e-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: 38.59 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 24 ERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRalydAELSQMQ 103
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR----AELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34069 104 THISDTSVVLSMDNNRNldldsiIAEVKAQYEEIAQRSRAEAesWYQTKYEELQvtagRHGDDLRNTKQEIAEINRMIQR 183
Cdd:COG4942 104 EELAELLRALYRLGRQP------PLALLLSPEDFLDAVRRLQ--YLKYLAPARR----EQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 34069 184 LRSESDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQEL 244
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| |
