|
Name |
Accession |
Description |
Interval |
E-value |
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
89-511 |
7.96e-159 |
|
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: 463.98 E-value: 7.96e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 89 RPMDELVTLEEA----DGGSDILLVVPKATVLQNQLDESQQERNDLMQL------------------KLQLEGQVTELRS 146
Cdd:pfam07888 1 KPLDELVTLEEEshgeEGGTDMLLVVPRAELLQNRLEECLQERAELLQAqeaanrqrekekerykrdREQWERQRRELES 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 147 RVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVK 226
Cdd:pfam07888 81 RVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 227 altreqeKLLGQLKEVQADKEQS----------------------------------------------------EAELE 254
Cdd:pfam07888 161 -------KAGAQRKEEEAERKQLqaklqqteeelrslskefqelrnslaqrdtqvlqlqdtittltqklttahrkEAENE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 255 PLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSV 334
Cdd:pfam07888 234 ALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 335 EAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEY 414
Cdd:pfam07888 314 EADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 415 MRKLEARLEKVADEKWNEDATTEDEEAavglscPAALTDSEDESPEDMRLPP----YGLCERG-----DPGSSPAGPREA 485
Cdd:pfam07888 394 IRQLEQRLETVADAKWSEAALTSTERP------DSPLSDSEDENPEALQPPRplghYSLCEQGqpdslLLATPPPSPRDP 467
|
490 500
....*....|....*....|....*.
gi 219521893 486 SPLVVISQPAPISPHlsgpaEDSSSD 511
Cdd:pfam07888 468 ESTVVISQPAPLSSP-----HQSSSD 488
|
|
| SKICH |
pfam17751 |
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ... |
15-87 |
1.15e-22 |
|
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The functions of the SKICH domains of NDP52 and CALCOCO1 are not known.
Pssm-ID: 465482 Cd Length: 102 Bit Score: 92.69 E-value: 1.15e-22
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219521893 15 VNFLNVARTYIPNTKVECHYTLPPGTMPSASDWIGIFKVEAACVRDYHTFVWssVPESTTDGSPIHTSVQFQE 87
Cdd:pfam17751 1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVW--AKDDEVEGSNSVRQVLFKA 71
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
112-451 |
1.89e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.69 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 112 KATVLQNQLDESQQErndLMQLKLQ-LEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQ 190
Cdd:COG1196 214 RYRELKEELKELEAE---LLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 191 GDHVARILELEDDIQTISEkvltkevELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASS 270
Cdd:COG1196 291 YELLAELARLEQDIARLEE-------RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 271 QQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKcqwsKERAGLLQSVEAEKDKILKLSAEILR 350
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL----ERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 351 LEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKW 430
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
330 340
....*....|....*....|.
gi 219521893 431 NEDATTEDEEAAVGLSCPAAL 451
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAAL 540
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
116-457 |
1.14e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 90.38 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVA 195
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 196 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKAT 275
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 276 LLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELglhlkeekcqwSKERAGLLQSVEAEKDKILKLSAEILRLEKAV 355
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAEL-----------EEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 356 QEERTQnqvfkTELAREkdsslvQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARL--EKVADEKWNED 433
Cdd:COG1196 466 AELLEE-----AALLEA------ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlaGAVAVLIGVEA 534
|
330 340
....*....|....*....|....
gi 219521893 434 ATTEDEEAAVGLSCPAALTDSEDE 457
Cdd:COG1196 535 AYEAALEAALAAALQNIVVEDDEV 558
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
141-446 |
3.00e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.23 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 141 VTELRSRVQELERALATARQ-----------EHTELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISE 209
Cdd:COG1196 195 LGELERQLEPLERQAEKAERyrelkeelkelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 210 KVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARD 289
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 290 RTIAELHRSRLEVAEVNGRLAELGLHLKEEKcqwsKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTEL 369
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELA----EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 219521893 370 AREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEAAVGLS 446
Cdd:COG1196 431 AELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
112-442 |
1.78e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.37 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 112 KATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQG 191
Cdd:COG1196 254 ELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 192 DHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQ 271
Cdd:COG1196 334 ELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 272 QKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELglhlkeekcqwSKERAGLLQSVEAEKDKILKLSAEILRL 351
Cdd:COG1196 414 ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL-----------EEEEEALLELLAELLEEAALLEAALAEL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 352 EKAVQEERTQnqvfkTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKqellEYMRKLEARLEKVADEKWN 431
Cdd:COG1196 483 LEELAEAAAR-----LLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEA----AYEAALEAALAAALQNIVV 553
|
330
....*....|.
gi 219521893 432 EDATTEDEEAA 442
Cdd:COG1196 554 EDDEVAAAAIE 564
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
134-419 |
3.61e-15 |
|
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: 79.34 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 134 KLQLEGQVTELRSRVQELERALATARQEHT-------ELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQT 206
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELSSLQSELRrienrldELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSS 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 207 ISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADK-----EQSEAELEPLKEQLRGAQELAASSQQKATLLGEEL 281
Cdd:TIGR02169 749 LEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 282 ASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHlKEEKCQWSKERAGLLQSVEAEKDkilKLSAEILRLEK--AVQEER 359
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK-KEELEEELEELEAALRDLESRLG---DLKKERDELEAqlRELERK 904
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 219521893 360 TQNQVFKTELAREKDSSL-VQLSESKRELTELRSALRVLQKEK------EQLQEEKQELLEYMRKLE 419
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELkAKLEALEEELSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEIRALE 971
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
112-426 |
7.81e-15 |
|
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: 78.17 E-value: 7.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 112 KATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYkgisrshgeiteerDILSRQQG 191
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI--------------EELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 192 DHVARILELEDDIQTISEKvltkeveLDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQ 271
Cdd:TIGR02168 292 ALANEISRLEQQKQILRER-------LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 272 QKAtllgEELASAAAARDRTIAELhrsrlevaevngrlaelglhlkeekcqwSKERAGLLQSVEAEKDKILKLSAEILRL 351
Cdd:TIGR02168 365 AEL----EELESRLEELEEQLETL----------------------------RSKVAQLELQIASLNNEIERLEARLERL 412
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219521893 352 EKAVQEERTQNQVFKTELAR-EKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVA 426
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
117-424 |
8.22e-15 |
|
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: 78.17 E-value: 8.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 117 QNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTElmeqykgISRSHGEITEERDILSRQQGDHVAR 196
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE-------LSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 197 ILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKATL 276
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 277 LGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQ---WSKERAGLLQSVEAEKDKILKLSAEILRLEK 353
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEleaLLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219521893 354 AVQEERTQNQVFKTELAREKdsslVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLE-YMRKLEARLEK 424
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLE----LRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEdDEEEARRRLKR 976
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
208-428 |
3.04e-14 |
|
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: 74.80 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 208 SEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAA 287
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 288 RDRTIAELhRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSV-EAEKDKILKLSA---EILRLEKAVQEERTQNQ 363
Cdd:COG4942 99 LEAQKEEL-AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaPARREQAEELRAdlaELAALRAELEAERAELE 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219521893 364 VFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADE 428
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Zn-C2H2_CALCOCO1 |
cd21967 |
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ... |
569-597 |
3.88e-14 |
|
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 1 (CALCOCO1) and similar proteins; CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). It is recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation CALCOCO1 acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. It is involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. It functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. In association with CCAR1, CALCOCO1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells. CALCOCO1 contains a C2H2-type zinc binding domain.
Pssm-ID: 412013 Cd Length: 29 Bit Score: 66.37 E-value: 3.88e-14
10 20
....*....|....*....|....*....
gi 219521893 569 KECPICKERFPAESDKDALEDHMDGHFFF 597
Cdd:cd21967 1 KECPICKERFPLECDKDALEDHIDSHFFF 29
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
116-421 |
4.16e-14 |
|
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: 75.86 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVA 195
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEA 789
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 196 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKAT 275
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 276 LLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKE-----EKCQWSKERAGL-LQSVEAEKDKILKLSAEIL 349
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSElrrelEELREKLAQLELrLEGLEVRIDNLQERLSEEY 949
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 350 RLEKAVQEERTQNQVFKTELAREKDSSL---------VQLsESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEA 420
Cdd:TIGR02168 950 SLTLEEAEALENKIEDDEEEARRRLKRLenkikelgpVNL-AAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
.
gi 219521893 421 R 421
Cdd:TIGR02168 1029 E 1029
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
116-411 |
3.08e-13 |
|
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: 73.18 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDL-----MQLKLQlEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQ 190
Cdd:TIGR02169 196 KRQQLERLRREREKAeryqaLLKEKR-EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 191 GDHVARILEL-EDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKE-------VQADKEQSEAELEPLKEQLRG 262
Cdd:TIGR02169 275 EELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKleaeidkLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 263 AQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAEL---GLHLKEEKCQWSKERAGLLQSVEAEKD 339
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELkreLDRLQEELQRLSEELADLNAAIAGIEA 434
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219521893 340 KILKLSAEILRLEKAVQEERTQNQVFKTELAREKdsslvqlseskRELTELRSALRVLQKEKEQLQEEKQEL 411
Cdd:TIGR02169 435 KINELEEEKEDKALEIKKQEWKLEQLAADLSKYE-----------QELYDLKEEYDRVEKELSKLQRELAEA 495
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
116-461 |
3.98e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITE---ERDILSRQQGD 192
Cdd:PRK02224 204 LHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAEterEREELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 193 HVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQ 272
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 273 KATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEkcqwSKERAGLLQSVEAEKDKILKLSAEILRLE 352
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA----EDFLEELREERDELREREAELEATLRTAR 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 353 KAVQEERTQNQVFKT-ELARE-KDSSLVQLSESKRE-LTELRSALRVLQKEKEQLqEEKQELLEYMRKLEARLEKVADEK 429
Cdd:PRK02224 440 ERVEEAEALLEAGKCpECGQPvEGSPHVETIEEDRErVEELEAELEDLEEEVEEV-EERLERAEDLVEAEDRIERLEERR 518
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 219521893 430 WN--------EDATTEDEEAAVGLSCPAALTDSEDESPED 461
Cdd:PRK02224 519 EDleeliaerRETIEEKRERAEELRERAAELEAEAEEKRE 558
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
116-441 |
4.99e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELR--SRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQgdh 193
Cdd:COG4717 93 LQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELE--- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 194 vARILELEDDIQTISEKV-LTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQ 272
Cdd:COG4717 170 -AELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 273 KATLLGE----------------------------------------ELASAAAARDRTIAELHRSRLEVAEVNGRLAEL 312
Cdd:COG4717 249 RLLLLIAaallallglggsllsliltiagvlflvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAAL 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 313 GL-----------------HLKEEKCQWSKERAGL-LQSVEAEKDKILKLS--------AEILRLEKAVQEERTQNQVFK 366
Cdd:COG4717 329 GLppdlspeellelldrieELQELLREAEELEEELqLEELEQEIAALLAEAgvedeeelRAALEQAEEYQELKEELEELE 408
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219521893 367 TELAREKDSSLVQLSESKREltELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEA 441
Cdd:COG4717 409 EQLEELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEEL 481
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
199-405 |
6.18e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.71 E-value: 6.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 199 ELEDDIQTISEkvltkevELDRLRDTVKAL--TREQEKLLGQLKEVQ---ADKEQSEAELEPLKEQLR--GAQELAASSQ 271
Cdd:COG4913 222 DTFEAADALVE-------HFDDLERAHEALedAREQIELLEPIRELAeryAAARERLAELEYLRAALRlwFAQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 272 QKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGL----HLKEEKCQWSKERAGLLQSVEAEKDKILKLSAE 347
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGdrleQLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 219521893 348 ILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQ 405
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
137-442 |
1.50e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 64.29 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 137 LEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEV 216
Cdd:PRK02224 256 LEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 217 ELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELH 296
Cdd:PRK02224 336 AAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLE 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 297 RSRLEVAEVNGRLAELGLHLKEEK-----------------CQWSKERAGLLQSVEAEKDKILKLSAEILRLEkaVQEER 359
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARerveeaealleagkcpeCGQPVEGSPHVETIEEDRERVEELEAELEDLE--EEVEE 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 360 TQNQVFKTELAREKDSSLVQLSESKRELTELRSalrvlqkEKEQLQEEKQELLEYMRKLEARLEKVADEKwnEDATTEDE 439
Cdd:PRK02224 494 VEERLERAEDLVEAEDRIERLEERREDLEELIA-------ERRETIEEKRERAEELRERAAELEAEAEEK--REAAAEAE 564
|
...
gi 219521893 440 EAA 442
Cdd:PRK02224 565 EEA 567
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
116-413 |
2.01e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 63.89 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTEL---MEQYKGISRSHGEITEERDILSRQQGd 192
Cdd:TIGR04523 150 KEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLellLSNLKKKIQKNKSLESQISELKKQNN- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 193 hvarilELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQ-ELAASSQ 271
Cdd:TIGR04523 229 ------QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKsEISDLNN 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 272 QKATLLGEELASAAAARDRTIAELhrsRLEVAEVNGRLAElglhLKEEKCQWSKERAGlLQSVEAEKDKilklsaEILRL 351
Cdd:TIGR04523 303 QKEQDWNKELKSELKNQEKKLEEI---QNQISQNNKIISQ----LNEQISQLKKELTN-SESENSEKQR------ELEEK 368
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219521893 352 EKAVQEERTQNQVFKTE---LAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLE 413
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEiknLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
|
| Zn-C2H2_12 |
pfam18112 |
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ... |
569-595 |
2.03e-10 |
|
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and coiled-coil domain 2/NDP25 (CALCOCO2/NDP25) found in Homo sapiens. CALCOCO2/NDP25 is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. This domain is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 407946 Cd Length: 27 Bit Score: 55.73 E-value: 2.03e-10
10 20
....*....|....*....|....*..
gi 219521893 569 KECPICKERFPAESDKDALEDHMDGHF 595
Cdd:pfam18112 1 KECPLCGEMFSPNIDQSEFEEHVESHF 27
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
85-424 |
8.90e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 8.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 85 FQEPRP-MDELVTLEEADGGSDILLVVPKATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHT 163
Cdd:PRK03918 364 YEEAKAkKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 164 ELMEQYKG--ISRSHGEIteeRDILSRqqgdhVARILELEDDIQ---TISEKVLTKEVELDRLRDTVKALTREQEKLLG- 237
Cdd:PRK03918 444 ELTEEHRKelLEEYTAEL---KRIEKE-----LKEIEEKERKLRkelRELEKVLKKESELIKLKELAEQLKELEEKLKKy 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 238 QLKEVQADKEQSE----------AELEPLKEQLRGAQELaassQQKATLLGEELASAaaarDRTIAELHRSRLE-----V 302
Cdd:PRK03918 516 NLEELEKKAEEYEklkekliklkGEIKSLKKELEKLEEL----KKKLAELEKKLDEL----EEELAELLKELEElgfesV 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 303 AEVNGRLAELG------LHLKEEKcqwsKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKdss 376
Cdd:PRK03918 588 EELEERLKELEpfyneyLELKDAE----KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE--- 660
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 219521893 377 lvqLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEK 424
Cdd:PRK03918 661 ---YEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
116-286 |
1.07e-09 |
|
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: 61.62 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVA 195
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 196 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQ-ELAASSQQKA 274
Cdd:TIGR02169 421 ELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQrELAEAEAQAR 500
|
170
....*....|..
gi 219521893 275 TLLGEELASAAA 286
Cdd:TIGR02169 501 ASEERVRGGRAV 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
141-443 |
2.19e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.84 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 141 VTELRSRVQELERALATARQEhtelMEQYKGIsrsHGEITEERDILSRQqGDHVARILELEDDIQTISEKVLTKEV---- 216
Cdd:TIGR02168 167 ISKYKERRKETERKLERTREN----LDRLEDI---LNELERQLKSLERQ-AEKAERYKELKAELRELELALLVLRLeelr 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 217 -ELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQ-ELAASSQQKATLLGEELasaaaardRTIAE 294
Cdd:TIGR02168 239 eELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkELYALANEISRLEQQKQ--------ILRER 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 295 LHRSRLEVAEVNGRLAELGLHLKEekcqwskeragLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTelarekd 374
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDE-----------LAEELAELEEKLEELKEELESLEAELEELEAELEELES------- 372
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 219521893 375 sslvQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEkwNEDATTEDEEAAV 443
Cdd:TIGR02168 373 ----RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQE--IEELLKKLEEAEL 435
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
97-417 |
3.03e-09 |
|
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: 60.24 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 97 LEEADGGSDILLVVPKATVLqnqldesQQERNDLMQLKLQLEGqvteLRSRVQELERALATARQEHTELMEQYKGISRS- 175
Cdd:pfam12128 227 IRDIQAIAGIMKIRPEFTKL-------QQEFNTLESAELRLSH----LHFGYKSDETLIASRQEERQETSAELNQLLRTl 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 176 HGEITEERDilsrqqgdhvarilELEDDIQTISEKVLTKEVELDRLRDTVKALTREQ-EKL---LGQLKEVQADKEQSEA 251
Cdd:pfam12128 296 DDQWKEKRD--------------ELNGELSAADAAVAKDRSELEALEDQHGAFLDADiETAaadQEQLPSWQSELENLEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 252 ELEPLKEQLRGAQE------LAASSQQKATLLG--EELASA--AAARDRTIAELHRSRLEvAEVNGRLAELGLHLKEEKC 321
Cdd:pfam12128 362 RLKALTGKHQDVTAkynrrrSKIKEQNNRDIAGikDKLAKIreARDRQLAVAEDDLQALE-SELREQLEAGKLEFNEEEY 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 322 QWsKERAG----LLQSVEAEKDKILKLSAEILRLEKAvQEERTQNQVFKTELARE-------KDSSLVQLSESKRELTEL 390
Cdd:pfam12128 441 RL-KSRLGelklRLNQATATPELLLQLENFDERIERA-REEQEAANAEVERLQSElrqarkrRDQASEALRQASRRLEER 518
|
330 340
....*....|....*....|....*..
gi 219521893 391 RSALRVLQkekEQLQEEKQELLEYMRK 417
Cdd:pfam12128 519 QSALDELE---LQLFPQAGTLLHFLRK 542
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
211-428 |
4.59e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 4.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 211 VLTKEVELDRLRDTVKALTREQEKLLGQLKEVqadkEQSEAELEPLKEQLR--GAQELAASSQQKATLLGEELASAAAAR 288
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAEL----RKELEELEEELEQLRkeLEELSRQISALRKDLARLEAEVEQLEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 289 DRTIAELHRSRLEV--AEVNGRLAELGLHLKEEKCQWSK---ERAGLLQSVEAEKDKILKLSAEI--LRLEKAVQEERTQ 361
Cdd:TIGR02168 748 RIAQLSKELTELEAeiEELEERLEEAEEELAEAEAEIEEleaQIEQLKEELKALREALDELRAELtlLNEEAANLRERLE 827
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219521893 362 NQVFK--------TELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADE 428
Cdd:TIGR02168 828 SLERRiaaterrlEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEE 902
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
143-463 |
4.74e-09 |
|
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: 59.47 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 143 ELRSRVQELERALATARQEHTELMEQYkgisrshGEITEERDILSRQQGDHVARILELEDDIQTISEKvltKEVELDRLR 222
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQL-------VQANGELEKASREETFARTALKNARLDLRRLFDE---KQSEKDKKN 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 223 dtvKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRG-AQELAASSQQKATLLGEELASAAAARDRTIAELHRSRle 301
Cdd:pfam12128 671 ---KALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEqKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGA-- 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 302 vaevngrlaelglhlKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAV-------QEERTQNQVFKTELAREKD 374
Cdd:pfam12128 746 ---------------KAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIeriavrrQEVLRYFDWYQETWLQRRP 810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 375 SSLVQLSESKRELTELRSALRVLQK---------EKEQLQEEKQ--ELLEYMRKLEARLEKVADEKWNEDATTEDEEAAV 443
Cdd:pfam12128 811 RLATQLSNIERAISELQQQLARLIAdtklrraklEMERKASEKQqvRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGE 890
|
330 340
....*....|....*....|
gi 219521893 444 GLSCPAALTDSEDESPEDMR 463
Cdd:pfam12128 891 RLAQLEDLKLKRDYLSESVK 910
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
112-287 |
4.86e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 4.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 112 KATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGI------------------- 172
Cdd:COG3883 31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsvsyldvllg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 173 SRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAE 252
Cdd:COG3883 111 SESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
170 180 190
....*....|....*....|....*....|....*
gi 219521893 253 LEPLKEQLRGAQELAASSQQKATLLGEELASAAAA 287
Cdd:COG3883 191 EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
112-293 |
1.15e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 112 KATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRS---HGEITEERDILSR 188
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRAlyrLGRQPPLALLLSP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 189 QQGDHVARIL-----------ELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELE-PL 256
Cdd:COG4942 129 EDFLDAVRRLqylkylaparrEQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEkEL 208
|
170 180 190
....*....|....*....|....*....|....*..
gi 219521893 257 KEQLRGAQELAASSQQKATLLGEELASAAAARDRTIA 293
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
112-312 |
1.58e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.08 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 112 KATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQG 191
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 192 DHVARILELEDDIQTISEKVLTKEV-------ELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQ 264
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLlspedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 219521893 265 ELAASSQQkatllgeELASAAAARDRTIAELHRSRLEVAEvngRLAEL 312
Cdd:COG4942 181 AELEEERA-------ALEALKAERQKLLARLEKELAELAA---ELAEL 218
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
116-443 |
2.06e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.44 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELM-------EQYKGISRSH------------ 176
Cdd:pfam15921 115 LQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLedsntqiEQLRKMMLSHegvlqeirsilv 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 177 ------GEITEERDILS----RQQGDHVARIL-ELEDDIQTISEKVLTKEVELdrlrDTVKALTREQEKLLGQLKEVQAD 245
Cdd:pfam15921 195 dfeeasGKKIYEHDSMStmhfRSLGSAISKILrELDTEISYLKGRIFPVEDQL----EALKSESQNKIELLLQQHQDRIE 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 246 KEQSEAELE--PLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELH------RSRLEVAE--VNGRLAELGLH 315
Cdd:pfam15921 271 QLISEHEVEitGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLEstvsqlRSELREAKrmYEDKIEELEKQ 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 316 L----------KEEKCQWSKERAGLlqsveaeKDKILKLSAEILRLEKAVQEERTQNqvfKTELAREKDSSLV------Q 379
Cdd:pfam15921 351 LvlanselteaRTERDQFSQESGNL-------DDQLQKLLADLHKREKELSLEKEQN---KRLWDRDTGNSITidhlrrE 420
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219521893 380 LSESKRELTELRSALRVLQKE-KEQLQEE------KQELLEYMRKLEARLE-------KVADEKWNEDATTEDEEAAV 443
Cdd:pfam15921 421 LDDRNMEVQRLEALLKAMKSEcQGQMERQmaaiqgKNESLEKVSSLTAQLEstkemlrKVVEELTAKKMTLESSERTV 498
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
119-429 |
2.41e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 119 QLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARqehtELMEQYKGIS-------RSHGEITEERDilsRQQG 191
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAE----ALLEAGKCPEcgqpvegSPHVETIEEDR---ERVE 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 192 DHVARILELEDDIQTISEKV--LTKEVELDRLRDTVkaltREQEKLLGQLKEVQADK-EQSEAELEPLKEQlrgAQELAA 268
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLerAEDLVEAEDRIERL----EERREDLEELIAERRETiEEKRERAEELRER---AAELEA 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 269 SSQQKAtllgeelASAAAARDRtiAELHRSrlEVAEVNGRLAELglhlkeekcqwsKERAGLLQSVEAEKDKILKLSAEI 348
Cdd:PRK02224 552 EAEEKR-------EAAAEAEEE--AEEARE--EVAELNSKLAEL------------KERIESLERIRTLLAAIADAEDEI 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 349 LRLekavQEERTQnqvfKTELAREKDSSLVQLSESKRELTELRSALRVlqkekEQLQEEKQELLEYMRKLEARLEKVADE 428
Cdd:PRK02224 609 ERL----REKREA----LAELNDERRERLAEKRERKRELEAEFDEARI-----EEAREDKERAEEYLEQVEEKLDELREE 675
|
.
gi 219521893 429 K 429
Cdd:PRK02224 676 R 676
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
137-442 |
3.02e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.85 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 137 LEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILS-----RQQGDHVARILELEDDIQTISEKV 211
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASaereiAELEAELERLDASSDDLAALEEQL 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 212 LTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAAssqqkATLLGEELASAAAARDRT 291
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL-----EERFAAALGDAVERELRE 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 292 IAELHRSRLEvAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEA--EKDKIL-KLSAEIL--RLEKAVQEERTQNQVFK 366
Cdd:COG4913 770 NLEERIDALR-ARLNRAEEELERAMRAFNREWPAETADLDADLESlpEYLALLdRLEEDGLpeYEERFKELLNENSIEFV 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 367 TELAREKDSSlvqLSESKRELTELRSALRVLQ-KEKEQLQ-----EEKQELLEYMRKLEArlekvadekWNEDATTEDEE 440
Cdd:COG4913 849 ADLLSKLRRA---IREIKERIDPLNDSLKRIPfGPGRYLRlearpRPDPEVREFRQELRA---------VTSGASLFDEE 916
|
..
gi 219521893 441 AA 442
Cdd:COG4913 917 LS 918
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
112-428 |
7.08e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.41 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 112 KATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALataRQEHTELmeqykgisrshgeITEERDILSRQQg 191
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL---EEKQNEI-------------EKLKKENQSYKQ- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 192 dhvaRILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQ 271
Cdd:TIGR04523 385 ----EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLD 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 272 QKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAElglhLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRL 351
Cdd:TIGR04523 461 NTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK----LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 352 EKAVQEERTQNQVFKTELAR-----EKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVA 426
Cdd:TIGR04523 537 ESKISDLEDELNKDDFELKKenlekEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
..
gi 219521893 427 DE 428
Cdd:TIGR04523 617 KE 618
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
119-295 |
7.18e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 119 QLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGIS-RSHGEITEERDILSRQQGDHVARI 197
Cdd:COG4913 282 RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 198 LELEDDIQTISEKVLTKEVELDRLRDTVKALtreQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKATLL 277
Cdd:COG4913 362 ARLEALLAALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNI 438
|
170
....*....|....*...
gi 219521893 278 GEELasaAAARDRTIAEL 295
Cdd:COG4913 439 PARL---LALRDALAEAL 453
|
|
| Zn-C2H2_CALCOCO1_TAX1BP1_like |
cd21965 |
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ... |
571-594 |
8.55e-08 |
|
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil domain-containing proteins, TAX1BP1 and similar proteins; The family includes calcium-binding and coiled-coil domain-containing proteins (CALCOCO1 and CALCOCO2), TAX1BP1 and similar proteins. CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. The family also includes Drosophila melanogaster Spindle-F (Spn-F) that is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. This model corresponds to the C2H2-type zinc binding domain found in family members. It is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.
Pssm-ID: 412012 Cd Length: 24 Bit Score: 48.34 E-value: 8.55e-08
10 20
....*....|....*....|....
gi 219521893 571 CPICKERFPAESDKDALEDHMDGH 594
Cdd:cd21965 1 CPICNKQFPPQVDQEAFEDHVESH 24
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
197-410 |
1.09e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 197 ILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQEL---AASSQQK 273
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREElgeRARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 274 ATLLGEELASAAAARDrtIAELHRSRLEVAEVNGRLAELGLHLKEEKcqwsKERAGLLQSVEAEKDKILKLSAEILRLEK 353
Cdd:COG3883 98 SGGSVSYLDVLLGSES--FSDFLDRLSALSKIADADADLLEELKADK----AELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 219521893 354 AVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQE 410
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
116-442 |
1.34e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVA 195
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 196 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQL--------------- 260
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALllaglrglagavavl 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 261 -------------------------------RGAQELAASSQQKATLLGEELASAAAARDRTIAEL-------------- 295
Cdd:COG1196 530 igveaayeaaleaalaaalqnivveddevaaAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGaigaavdlvasdlr 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 296 -HRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKD 374
Cdd:COG1196 610 eADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 219521893 375 SSLVQLSESKRELTELRSALRV---------LQKEKEQLQEEKQELLEYMRKLEARLEKVADEKwNEDATTEDEEAA 442
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEaeeerleeeLEEEALEEQLEAEREELLEELLEEEELLEEEAL-EELPEPPDLEEL 765
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
116-270 |
1.81e-07 |
|
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: 52.62 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQgdhva 195
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQK----- 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219521893 196 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASS 270
Cdd:COG1579 97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
133-312 |
1.87e-07 |
|
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: 52.23 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 133 LKLQlegqvtELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQqgdhvarILELEDDIQTISEKVL 212
Cdd:COG1579 10 LDLQ------ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKE-------IKRLELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 213 TKEVELDRLRDtvkalTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTI 292
Cdd:COG1579 77 KYEEQLGNVRN-----NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL 151
|
170 180
....*....|....*....|
gi 219521893 293 AELHRsrlEVAEVNGRLAEL 312
Cdd:COG1579 152 AELEA---ELEELEAEREEL 168
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
114-295 |
1.93e-07 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 53.22 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 114 TVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALA----TARQEHTELMEQYKGISRSHGEITEE------- 182
Cdd:pfam09787 43 TALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQeeaeSSREQLQELEEQLATERSARREAEAElerlqee 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 183 ----RDILSRQQGDHVARILELEDDIQTISEKVLTK------EVELD-RLRDTVKALTREQEkllgQLKEVQADKEQSEA 251
Cdd:pfam09787 123 lrylEEELRRSKATLQSRIKDREAEIEKLRNQLTSKsqssssQSELEnRLHQLTETLIQKQT----MLEALSTEKNSLVL 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 219521893 252 ELEPLKEQLRGAQelaASSQQKATLLGEELASAAAARDRTIAEL 295
Cdd:pfam09787 199 QLERMEQQIKELQ---GEGSNGTSINMEGISDGEGTRLRNVPGL 239
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
152-350 |
4.22e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 152 ERALATARQEHTELMEQYKGISRSHGEITEERDILsRQQGDHVARILEL---EDDIQTISEKVLTKEVELDRLR---DTV 225
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDAL-QERREALQRLAEYswdEIDVASAEREIAELEAELERLDassDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 226 KALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKAtllgEELASAAAARDRTIAELHRSRLEVAEV 305
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL----EAAEDLARLELRALLEERFAAALGDAV 763
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 219521893 306 NGRLAElglhlkeekcQWSKERAGLLQSVEAEKDKILKLSAEILR 350
Cdd:COG4913 764 ERELRE----------NLEERIDALRARLNRAEEELERAMRAFNR 798
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
116-422 |
4.31e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQ-LEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQ---- 190
Cdd:COG4717 175 LQEELEELLEQLSLATEEELQdLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLllli 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 191 ----------GDH--------------VARILELEDDIQTISEKVLTKEVELDRLRDTVKALtrEQEKLLGQLKEVQADK 246
Cdd:COG4717 255 aaallallglGGSllsliltiagvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEEL--EEEELEELLAALGLPP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 247 EQSEAELEPLKEQLRGAQELAAS-------------SQQKATLLGE----------ELASAAAARDRTIAELHRSRLEVA 303
Cdd:COG4717 333 DLSPEELLELLDRIEELQELLREaeeleeelqleelEQEIAALLAEagvedeeelrAALEQAEEYQELKEELEELEEQLE 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 304 EVNGRLAELGLHLKEEkcQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVfkTELAREKDSSLVQLSES 383
Cdd:COG4717 413 ELLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL--AELLQELEELKAELREL 488
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 219521893 384 KRELTELRSALRVLQKEKEQLQEEKQ-ELLEYMRKLEARL 422
Cdd:COG4717 489 AEEWAALKLALELLEEAREEYREERLpPVLERASEYFSRL 528
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
199-440 |
7.39e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 52.36 E-value: 7.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 199 ELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGA----QELAASSQQKA 274
Cdd:TIGR00606 692 ELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVnrdiQRLKNDIEEQE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 275 TLLGEELASAAAARD--RTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERagLLQSVEAEKDKILKLSAEILRLE 352
Cdd:TIGR00606 772 TLLGTIMPEEESAKVclTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQ--VNQEKQEKQHELDTVVSKIELNR 849
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 353 KAVQEERTQNQVFKTELaREKDSSLVQLSEskreltelrsALRVLQKEKEQLQEEKQELLEYMRKL-EARLEKVADEKWN 431
Cdd:TIGR00606 850 KLIQDQQEQIQHLKSKT-NELKSEKLQIGT----------NLQRRQQFEEQLVELSTEVQSLIREIkDAKEQDSPLETFL 918
|
....*....
gi 219521893 432 EDATTEDEE 440
Cdd:TIGR00606 919 EKDQQEKEE 927
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
125-439 |
7.85e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 7.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 125 QERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDI 204
Cdd:PRK02224 314 ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 205 QTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVqadkeqsEAELEPLKEQLRGAQEL------------------ 266
Cdd:PRK02224 394 EELRERFGDAPVDLGNAEDFLEELREERDELREREAEL-------EATLRTARERVEEAEALleagkcpecgqpvegsph 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 267 ---AASSQQKATLLGEELASAAAARDRTIAELHRSRlEVAEVNGRLAEL----------------GLHLKEEKCQWSKER 327
Cdd:PRK02224 467 vetIEEDRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLeerredleeliaerreTIEEKRERAEELRER 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 328 AGLLQSVEAEKDkilklsAEILRLEKAVQEERTQNQVFKTELAREKDS--SLVQLSESKRELTELRSALRVLQKEKEQLQ 405
Cdd:PRK02224 546 AAELEAEAEEKR------EAAAEAEEEAEEAREEVAELNSKLAELKERieSLERIRTLLAAIADAEDEIERLREKREALA 619
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 219521893 406 EEKQELLEYM-------RKLEARLEKVADEKWNEDATTEDE 439
Cdd:PRK02224 620 ELNDERRERLaekrerkRELEAEFDEARIEEAREDKERAEE 660
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
225-429 |
8.15e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 8.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 225 VKALTREQEKLLgqlKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKAtllgEELASAAAARDRTIAELHRSRLEVAE 304
Cdd:COG4717 48 LERLEKEADELF---KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQ----EELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 305 VNGRLAELGLHLKEEKCQwsKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESK 384
Cdd:COG4717 121 LEKLLQLLPLYQELEALE--AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 219521893 385 RELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEK 429
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
118-417 |
8.33e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 8.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 118 NQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARI 197
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 198 LELEDDIQTISEKVLTKEVELDRLRD---TVKALTREQEKLLGQLKEVQADKEQSE---AELEPLKEQLRGAQELAASSQ 271
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKaggSIDKLRKEIERLEWRQQTEVLSPEEEKelvEKIKELEKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 272 QKATLLgeelasaaaardrtiAELHRSRLEVAEVNGRLAELGlhlkEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRL 351
Cdd:COG1340 161 KLKELR---------------AELKELRKEAEEIHKKIKELA----EEAQELHEEMIELYKEADELRKEADELHKEIVEA 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219521893 352 EKAVQEERTQnqvfktelareKDSSLVQLSESKRELTELRSALRVLQKEKEQ--LQEEKQELLEYMRK 417
Cdd:COG1340 222 QEKADELHEE-----------IIELQKELRELRKELKKLRKKQRALKREKEKeeLEEKAEEIFEKLKK 278
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
147-421 |
1.09e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 147 RVQELERA---LATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKV--LTKEV-ELDR 220
Cdd:PRK03918 156 GLDDYENAyknLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELekLEKEVkELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 221 LRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSqqkatllgEELASAAAARDRTIAELHRSRL 300
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL--------KELKEKAEEYIKLSEFYEEYLD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 301 EVAEVNGRLAELglhlkEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRlEKAVQEERTQnqvfKTELAREKDSSLVQL 380
Cdd:PRK03918 308 ELREIEKRLSRL-----EEEINGIEERIKELEEKEERLEELKKKLKELEK-RLEELEERHE----LYEEAKAKKEELERL 377
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 219521893 381 SESKRELT--ELRSALRVLQKEKEQLQEEKQELLEYMRKLEAR 421
Cdd:PRK03918 378 KKRLTGLTpeKLEKELEELEKAKEEIEEEISKITARIGELKKE 420
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
117-410 |
1.60e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 51.36 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 117 QNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHvAR 196
Cdd:pfam10174 464 RERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQL-KK 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 197 ILELEDDIQT---ISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQA---DKEQSEAELEPL-----KEQLRGAQE 265
Cdd:pfam10174 543 AHNAEEAVRTnpeINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVENeknDKDKKIAELESLtlrqmKEQNKKVAN 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 266 LAASSQQKATLLGEELASAAAARDRTIAELHRSRLEvaEVNGRLAELGLHLKEekcqwSKERAGLLQSVEAEKDKILkls 345
Cdd:pfam10174 623 IKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLE--ELMGALEKTRQELDA-----TKARLSSTQQSLAEKDGHL--- 692
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 346 aEILRLEKAVQEERTQNQVFKTELA--REKDS--SLVQLSESKRELTELRSALrvLQKEKEQL-QEEKQE 410
Cdd:pfam10174 693 -TNLRAERRKQLEEILEMKQEALLAaiSEKDAniALLELSSSKKKKTQEEVMA--LKREKDRLvHQLKQQ 759
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
116-424 |
1.99e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYK----------------GISRSHGEI 179
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAdyegflegvkaalllaGLRGLAGAV 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 180 TEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRL----RDTVKALTREQEKLLGQLKEVQADKEQSEAELEP 255
Cdd:COG1196 527 AVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAakagRATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 256 LKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEkcqwSKERAGLLQSVE 335
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL----LAALLEAEAELE 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 336 AEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYM 415
Cdd:COG1196 683 ELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
....*....
gi 219521893 416 RKLEARLEK 424
Cdd:COG1196 763 EELERELER 771
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
200-409 |
3.56e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 200 LEDDIQTISEKVLTKEVELDRLRDTVK--ALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQkatll 277
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD----- 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 278 geelASAAAARDRTIAELhrsRLEVAEVNGRLAELGLHLKEE-----KCQwsKERAGLLQSVEAEKDKIL-KLSAEILRL 351
Cdd:COG3206 255 ----ALPELLQSPVIQQL---RAQLAELEAELAELSARYTPNhpdviALR--AQIAALRAQLQQEAQRILaSLEAELEAL 325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 219521893 352 EKAVQEERTQNQVFKTELAREKDSSlVQLSESKRELTELRSALRVLQKEKEQLQEEKQ 409
Cdd:COG3206 326 QAREASLQAQLAQLEARLAELPELE-AELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
204-440 |
4.02e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 204 IQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKATLLGEELAS 283
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 284 AAAARDRTIAELHRSRLEVAEvngrlaelglhLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQ 363
Cdd:COG4372 106 LQEEAEELQEELEELQKERQD-----------LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 219521893 364 VFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEE 440
Cdd:COG4372 175 ALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
215-514 |
6.14e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 6.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 215 EVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAE 294
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 295 LHRSRLEVAEVNgrlAELGlhlkeekcqwSKERAGLLQSVEAeKDKILKLSAEILRLEKAVQEErtqnqvfkteLAREKD 374
Cdd:COG3883 95 LYRSGGSVSYLD---VLLG----------SESFSDFLDRLSA-LSKIADADADLLEELKADKAE----------LEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 375 sslvQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEAAVGLSCPAALTDS 454
Cdd:COG3883 151 ----ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 455 EDESPEDMRLPPYGLCERGDPGSSPAGPREASPLVVISQPAPISPHLSGPAEDSSSDSEA 514
Cdd:COG3883 227 AAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGA 286
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
201-511 |
6.42e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 6.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 201 EDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLrgaQELAASSQQKATLLGEE 280
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI---AEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 281 LASAAAARDRTiaelhrSRLEVAEVNGRLAELglhlkeekcqwsKERAGLLQSVEAEKDKILKlsaEILRLEKAVQEERT 360
Cdd:COG3883 92 ARALYRSGGSV------SYLDVLLGSESFSDF------------LDRLSALSKIADADADLLE---ELKADKAELEAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 361 QNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKwneDATTEDEE 440
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA---AAAAAAAA 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219521893 441 AAVGLSCPAALTDSEDESPEDMRLPPYGLCERGDPGSSPAGPREASPLVVISQPAPISPHLSGPAEDSSSD 511
Cdd:COG3883 228 AAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGA 298
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
208-441 |
7.56e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 7.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 208 SEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAA 287
Cdd:PTZ00121 1499 ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNM 1578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 288 RDRTIAELHRSRLEVAEVNGRLAELGLHLKEE---KCQWSKERAGLLQSVEAEKDKILKLS---AEILRLEKAVQEERTQ 361
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEeakKAEEAKIKAEELKKAEEEKKKVEQLKkkeAEEKKKAEELKKAEEE 1658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 362 NQVFKTELAREKDsslvqlsESKRELTELRSALRVLQKEKEQLQEEKQEL--LEYMRKLEARLEKVADE--KWNEDATTE 437
Cdd:PTZ00121 1659 NKIKAAEEAKKAE-------EDKKKAEEAKKAEEDEKKAAEALKKEAEEAkkAEELKKKEAEEKKKAEElkKAEEENKIK 1731
|
....
gi 219521893 438 DEEA 441
Cdd:PTZ00121 1732 AEEA 1735
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
114-421 |
7.99e-06 |
|
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: 49.02 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 114 TVLQNQLD-------ESQQERNDLMQLKLQLEGQVTELRSRVQELERalaTARQEHTELMEQYKGISRSHGEITEERDIL 186
Cdd:pfam01576 43 NALQEQLQaetelcaEAEEMRARLAARKQELEEILHELESRLEEEEE---RSQQLQNEKKKMQQHIQDLEEQLDEEEAAR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 187 SRQQGDHV---ARILELEDDIQTISEK--VLTKEVEL--DRLRDTVKALTREQEKL--LGQLK----------------- 240
Cdd:pfam01576 120 QKLQLEKVtteAKIKKLEEDILLLEDQnsKLSKERKLleERISEFTSNLAEEEEKAksLSKLKnkheamisdleerlkke 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 241 -----EVQADKEQSEAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLH 315
Cdd:pfam01576 200 ekgrqELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQED 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 316 LKEEKCQWS---KERAGLLQSVEAEKDKIL--------------KLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLV 378
Cdd:pfam01576 280 LESERAARNkaeKQRRDLGEELEALKTELEdtldttaaqqelrsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALE 359
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 219521893 379 QLSEskrELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEAR 421
Cdd:pfam01576 360 ELTE---QLEQAKRNKANLEKAKQALESENAELQAELRTLQQA 399
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
124-424 |
8.29e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.27 E-value: 8.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 124 QQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEE------RDILSRQQGDHVARI 197
Cdd:TIGR00606 507 QNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnKKQLEDWLHSKSKEI 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 198 LELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVqADKEQSEAELEPLKEQLRGAQE----LAASS--- 270
Cdd:TIGR00606 587 NQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDV-CGSQDEESDLERLKEEIEKSSKqramLAGATavy 665
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 271 QQKATLLGEELASAAAARDRTIaelhRSRLEVAEVNGRLAELGLHLKEEKcqwsKERAGLLQSVEAEKDKILKL----SA 346
Cdd:TIGR00606 666 SQFITQLTDENQSCCPVCQRVF----QTEAELQEFISDLQSKLRLAPDKL----KSTESELKKKEKRRDEMLGLapgrQS 737
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219521893 347 EILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSAlRVLQKEKEQLQEEKQELLEYMRKLEARLEK 424
Cdd:TIGR00606 738 IIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESA-KVCLTDVTIMERFQMELKDVERKIAQQAAK 814
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
117-440 |
9.88e-06 |
|
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: 48.81 E-value: 9.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 117 QNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALataRQEHTELMEQYKGISrsHGEITEERDILSRQQGDhvaR 196
Cdd:pfam02463 703 KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLL---KQKIDEEEEEEEKSR--LKKEEKEEEKSELSLKE---K 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 197 ILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLR----GAQELAASSQQ 272
Cdd:pfam02463 775 ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELAlelkEEQKLEKLAEE 854
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 273 KATLLGEELASAA------AARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKIL-KLS 345
Cdd:pfam02463 855 ELERLEEEITKEEllqellLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILlKYE 934
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 346 AEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQK-------EKEQLQEEKQELLEYMRKL 418
Cdd:pfam02463 935 EEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEErynkdelEKERLEEEKKKLIRAIIEE 1014
|
330 340
....*....|....*....|..
gi 219521893 419 EARLEKVADEKWNEDATTEDEE 440
Cdd:pfam02463 1015 TCQRLKEFLELFVSINKGWNKV 1036
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
118-363 |
1.36e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.50 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 118 NQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGdhvari 197
Cdd:pfam15905 73 KDQKELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFS------ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 198 lelEDDIQtisEKVLTKEVELDRLRDTVKALTRE----QEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQK 273
Cdd:pfam15905 147 ---EDGTQ---KKMSSLSMELMKLRNKLEAKMKEvmakQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 274 ATLLGEELASAAAARDrtiaELHRSRLEVAEVNGRLAE-------LGLHLKEEKCQWSK---ERAGLLQSVEAEKDKILK 343
Cdd:pfam15905 221 TEKLLEYITELSCVSE----QVEKYKLDIAQLEELLKEkndeiesLKQSLEEKEQELSKqikDLNEKCKLLESEKEELLR 296
|
250 260
....*....|....*....|....*...
gi 219521893 344 --------LSAEILRLEKAVQEERTQNQ 363
Cdd:pfam15905 297 eyeekeqtLNAELEELKEKLTLEEQEHQ 324
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
140-423 |
1.47e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 140 QVTELRSRVQELERALATARQEHTELMEQykgISRSHGEITEERDILSRQQgdhvARILELEDDIQTISEKVLTKEVELD 219
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREE---LEQLEEELEQARSELEQLE----EELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 220 RLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSR 299
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 300 LE--VAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSL 377
Cdd:COG4372 185 LDelLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 219521893 378 VQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLE 423
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLI 310
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
120-417 |
1.73e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 120 LDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQ-----EHTELMEQYKGISRSHGEITEERDILSRQQGDhv 194
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRierleERREDLEELIAERRETIEEKRERAEELRERAA-- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 195 arilELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKL------LGQLKEVQADKEQSEAELEPLKEQLRGAQELAA 268
Cdd:PRK02224 548 ----ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELkeriesLERIRTLLAAIADAEDEIERLREKREALAELND 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 269 SSQqkatllgEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKcqwskeraglLQSVEAEKDKILKlsaEI 348
Cdd:PRK02224 624 ERR-------ERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEK----------LDELREERDDLQA---EI 683
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 219521893 349 LRLEKAVQEertqnqvfktelarekdssLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRK 417
Cdd:PRK02224 684 GAVENELEE-------------------LEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQ 733
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
86-384 |
1.93e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.81 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 86 QEPRPMDELVTLEEADGGSdilLVVPKATvLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERalatarqEHTEL 165
Cdd:pfam15921 569 QQIENMTQLVGQHGRTAGA---MQVEKAQ-LEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLEL-------EKVKL 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 166 MEQYKGISRSHGEITEERDILsrqqgdhVARILELEDDIQTISEKVltkEVELDRLRDTVKALTREQEKLLGQLKEVQAD 245
Cdd:pfam15921 638 VNAGSERLRAVKDIKQERDQL-------LNEVKTSRNELNSLSEDY---EVLKRNFRNKSEEMETTTNKLKMQLKSAQSE 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 246 KEQSEAELEPLKEQLRGAQELAASSQQKATllgeelasaaaARDRTIAELhRSRLEVAEVNGRLAELGLH-LKEEKCQWS 324
Cdd:pfam15921 708 LEQTRNTLKSMEGSDGHAMKVAMGMQKQIT-----------AKRGQIDAL-QSKIQFLEEAMTNANKEKHfLKEEKNKLS 775
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 325 KEraglLQSVEAEKDKILKlSAEILRlekaVQEERTQNQVFKTELAREKDSslVQLSESK 384
Cdd:pfam15921 776 QE----LSTVATEKNKMAG-ELEVLR----SQERRLKEKVANMEVALDKAS--LQFAECQ 824
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
219-420 |
2.04e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 219 DRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQlrgaqelaassqQKATLLGEELASAAAARDRTIAELHRS 298
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQK------------NGLVDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 299 RLEVAEVNGRLAELGLHLKEEkcqwSKERAGLLQS--VEAEKDKILKLSAEILRLEK-------AVQEERTQNQVFKTEL 369
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSG----PDALPELLQSpvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQL 307
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 219521893 370 AREKDSSLV----QLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEA 420
Cdd:COG3206 308 QQEAQRILAsleaELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV 362
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
120-432 |
2.68e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 120 LDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQ--EHTELMEQYKGISRSHGEI--------TEERDILSRQ 189
Cdd:PRK03918 454 LEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLKKYnleelekkAEEYEKLKEK 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 190 QGDHVARILELEDDIQTISEkvLTKEVELdrLRDTVKALTREQEKLLGQLKEVQ-ADKEQSEAELEPLKEQLRGAQELAA 268
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEE--LKKKLAE--LEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKD 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 269 SSQQKATLLGEelasaaaaRDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERagllqsVEAEKDKILKLSAEI 348
Cdd:PRK03918 610 AEKELEREEKE--------LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE------YEELREEYLELSREL 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 349 LRLEKAVQEERTQNQvfktelarEKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLE----ARLEK 424
Cdd:PRK03918 676 AGLRAELEELEKRRE--------EIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKeralSKVGE 747
|
....*...
gi 219521893 425 VADEKWNE 432
Cdd:PRK03918 748 IASEIFEE 755
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
116-425 |
2.90e-05 |
|
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: 47.09 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISrshGEITEERDILSRQQGDHVA 195
Cdd:pfam01576 248 ALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALK---TELEDTLDTTAAQQELRSK 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 196 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEP----LKEQLRGAQELAASSQ 271
Cdd:pfam01576 325 REQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESenaeLQAELRTLQQAKQDSE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 272 QKATLLG---EELASAAAARDRTIAEL----HRSRLEVAEVNGRLAELglhlkEEKC-QWSKERAGL---LQSVEA---- 336
Cdd:pfam01576 405 HKRKKLEgqlQELQARLSESERQRAELaeklSKLQSELESVSSLLNEA-----EGKNiKLSKDVSSLesqLQDTQEllqe 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 337 EKDKILKLSAEILRLEK---AVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLE 413
Cdd:pfam01576 480 ETRQKLNLSTRLRQLEDernSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQ 559
|
330
....*....|..
gi 219521893 414 YMRKLEARLEKV 425
Cdd:pfam01576 560 QLEEKAAAYDKL 571
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
290-443 |
3.72e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 290 RTIAELHRSRLEVAEVNGRLAELGLHLKEEKcqwsKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTEL 369
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAELAELE----DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 219521893 370 -----AREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEAAV 443
Cdd:COG1579 83 gnvrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
116-432 |
3.90e-05 |
|
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: 46.89 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRsrvqeLERALATARQEHTELMEQYKGISRSHGEITEERdilsrqqgdHVA 195
Cdd:TIGR00618 228 LKHLREALQQTQQSHAYLTQKREAQEEQLK-----KQQLLKQLRARIEELRAQEAVLEETQERINRAR---------KAA 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 196 RILEleddiqtISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADkEQSEAELEPLKEQLRGAQELAASSQQKAT 275
Cdd:TIGR00618 294 PLAA-------HIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQ-QSSIEEQRRLLQTLHSQEIHIRDAHEVAT 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 276 LLGEELasaaaarDRTIAELHRSRlevaevngRLAELGLHLKEEkcqwSKERAGLLQSVEAEKDKILKLSAEILRLEKAV 355
Cdd:TIGR00618 366 SIREIS-------CQQHTLTQHIH--------TLQQQKTTLTQK----LQSLCKELDILQREQATIDTRTSAFRDLQGQL 426
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 219521893 356 QEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNE 432
Cdd:TIGR00618 427 AHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP 503
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
138-407 |
3.91e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 138 EGQVTELRSRVQELERALATARQEHTELMEQYKgisrshgEITEERDILSRqqgdHVARILELEDDiqTISEKVLTKEVE 217
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLE-------QAKEGLSALNR----LLPRLNLLADE--TLADRVEEIREQ 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 218 LDRLRDTvKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKATLLGEELASAAA----------A 287
Cdd:PRK04863 903 LDEAEEA-KRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHfsyedaaemlA 981
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 288 RDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKC-QWSKERAGLLQSVEAEKDKILKLSAEILRL---------EKAVQE 357
Cdd:PRK04863 982 KNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLaQYNQVLASLKSSYDAKRQMLQELKQELQDLgvpadsgaeERARAR 1061
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 219521893 358 ERTQNQVFKTELAReKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEE 407
Cdd:PRK04863 1062 RDELHARLSANRSR-RNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQ 1110
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
231-422 |
5.40e-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: 44.92 E-value: 5.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 231 EQEKLLgQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAardrtiaELHRSRLEVAEVNGRLA 310
Cdd:COG1579 5 DLRALL-DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK-------EIKRLELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 311 ELGLHLKEEKCQwsKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDsslvqlsESKRELTEL 390
Cdd:COG1579 77 KYEEQLGNVRNN--KEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEA-------ELEEKKAEL 147
|
170 180 190
....*....|....*....|....*....|..
gi 219521893 391 RSALRVLQKEKEQLQEEKQELLEymrKLEARL 422
Cdd:COG1579 148 DEELAELEAELEELEAEREELAA---KIPPEL 176
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
221-433 |
7.67e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 221 LRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRL 300
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 301 EV--AEVNGRLAELGLhlKEEKCQWSKERAGLLQSVEAEK-DKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDssl 377
Cdd:PTZ00121 1666 EAkkAEEDKKKAEEAK--KAEEDEKKAAEALKKEAEEAKKaEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE--- 1740
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 219521893 378 vqlsESKRELTELRsalrVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNED 433
Cdd:PTZ00121 1741 ----EDKKKAEEAK----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEE 1788
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
208-312 |
8.07e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.96 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 208 SEKVLTKEVELDRLRDTVKALTR----EQEK---LLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKATLLGEE 280
Cdd:PRK09039 45 SREISGKDSALDRLNSQIAELADllslERQGnqdLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQE 124
|
90 100 110
....*....|....*....|....*....|..
gi 219521893 281 LASAAAARDRTIAELHRSRLEVAEVNGRLAEL 312
Cdd:PRK09039 125 LDSEKQVSARALAQVELLNQQIAALRRQLAAL 156
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
118-290 |
8.15e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 118 NQLDESQQERNDLMQLKLQ-LEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQgDHVAR 196
Cdd:PRK02224 522 EELIAERRETIEEKRERAEeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIR-TLLAA 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 197 ILELEDDIQTISEKVLTKEVELDRLRDTVKALtREQEKLLG------QLKEVQADKEQSEAELEPLKEQLRGAQELAASS 270
Cdd:PRK02224 601 IADAEDEIERLREKREALAELNDERRERLAEK-RERKRELEaefdeaRIEEAREDKERAEEYLEQVEEKLDELREERDDL 679
|
170 180
....*....|....*....|
gi 219521893 271 QQKATLLGEELASAAAARDR 290
Cdd:PRK02224 680 QAEIGAVENELEELEELRER 699
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
126-457 |
8.30e-05 |
|
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: 45.87 E-value: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 126 ERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARILEL--EDD 203
Cdd:pfam05483 416 EDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELtaHCD 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 204 IQTISEKVLTKE-----VELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAA----SSQQKA 274
Cdd:pfam05483 496 KLLLENKELTQEasdmtLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKckldKSEENA 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 275 TLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERagllQSVEAEKDKILKLSaeiLRLEKA 354
Cdd:pfam05483 576 RSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAEN----KQLNAYEIKVNKLE---LELASA 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 355 VQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDA 434
Cdd:pfam05483 649 KQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSELG 728
|
330 340
....*....|....*....|....*.
gi 219521893 435 ---TTEDEEAAVGLSCPAALTDSEDE 457
Cdd:pfam05483 729 lykNKEQEQSSAKAALEIELSNIKAE 754
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
143-428 |
8.58e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 8.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 143 ELRSRVQELERALATARQEHTElmEQYKgisrsHGEITEERDILSRQQGDhvarileLEDDIQTISE---KVLT---KEV 216
Cdd:COG3096 282 ELSERALELRRELFGARRQLAE--EQYR-----LVEMARELEELSARESD-------LEQDYQAASDhlnLVQTalrQQE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 217 ELDRLRDTVKALT---REQEKLL----GQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKAtlLGEELASAAAARD 289
Cdd:COG3096 348 KIERYQEDLEELTerlEEQEEVVeeaaEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRA--IQYQQAVQALEKA 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 290 RTIAELhrSRLEVAEVNGRLAELGLHLKE--EKCQWSKERAGLLQSVEAEKDKILKLsaeilrLEKAVQE-ERTQNQVFK 366
Cdd:COG3096 426 RALCGL--PDLTPENAEDYLAAFRAKEQQatEEVLELEQKLSVADAARRQFEKAYEL------VCKIAGEvERSQAWQTA 497
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219521893 367 TEL---AREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQE----------EKQELLEYMRKLEARLEKVADE 428
Cdd:COG3096 498 RELlrrYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEfcqrigqqldAAEELEELLAELEAQLEELEEQ 572
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
116-424 |
1.13e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.10 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRqqgdhva 195
Cdd:pfam05483 224 IQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTK------- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 196 rilELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQK-- 273
Cdd:pfam05483 297 ---ELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRle 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 274 -----ATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKcQWSK----------ERAGLLQSVEAEk 338
Cdd:pfam05483 374 knedqLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK-QFEKiaeelkgkeqELIFLLQAREKE- 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 339 dkILKLSAEILRLEKAVQEERTQNQVFKTELAREK------DSSLVQLSESKRELTELRSALRV-LQKEKEQLQEEKQEL 411
Cdd:pfam05483 452 --IHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKlknielTAHCDKLLLENKELTQEASDMTLeLKKHQEDIINCKKQE 529
|
330
....*....|...
gi 219521893 412 LEYMRKLEARLEK 424
Cdd:pfam05483 530 ERMLKQIENLEEK 542
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
195-348 |
1.18e-04 |
|
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: 43.76 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 195 ARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQL---RGAQELAASSQ 271
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQK 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 219521893 272 QKATlLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEI 348
Cdd:COG1579 97 EIES-LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
173-428 |
1.23e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 173 SRSHGEITEERDILSRQQ--GDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKL--LGQLKEVQADKEQ 248
Cdd:COG4913 586 NGTRHEKDDRRRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALqrLAEYSWDEIDVAS 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 249 SEAELEPLKEQLRgaqELAASSQQKATlLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELglhlkEEKCQWSKERa 328
Cdd:COG4913 666 AEREIAELEAELE---RLDASSDDLAA-LEEQLEELEAELEELEEELDELKGEIGRLEKELEQA-----EEELDELQDR- 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 329 glLQSVEAEKDKILKLSAEiLRLEKAVQEERTQnqvfktELAREKDSSLVQLsesKRELTELRSALRVLQKE-KEQLQEE 407
Cdd:COG4913 736 --LEAAEDLARLELRALLE-ERFAAALGDAVER------ELRENLEERIDAL---RARLNRAEEELERAMRAfNREWPAE 803
|
250 260
....*....|....*....|....
gi 219521893 408 KQEL---LEYMRKLEARLEKVADE 428
Cdd:COG4913 804 TADLdadLESLPEYLALLDRLEED 827
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
116-421 |
1.36e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.83 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATAR--------------QEHTELMEQYKGISRShGEITE 181
Cdd:PRK04778 117 IEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRfsfgpaldelekqlENLEEEFSQFVELTES-GDYVE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 182 ERDILSRQQgdhvARILELEDDIQTISE--KVLTKEV--ELDRLRDTVKALTRE-----QEKLLGQLKEVQADKEQSEAE 252
Cdd:PRK04778 196 AREILDQLE----EELAALEQIMEEIPEllKELQTELpdQLQELKAGYRELVEEgyhldHLDIEKEIQDLKEQIDENLAL 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 253 LEPLKeqLRGAQELAASSQQKATLLGEELASAAAARDrtiaelhrsrlEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQ 332
Cdd:PRK04778 272 LEELD--LDEAEEKNEEIQERIDQLYDILEREVKARK-----------YVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQ 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 333 SV---EAEKDKILKLSAEILRLEKAVQE--ERT--QNQVFkTELAREKDSSLVQLSESKRELTELRSALRVLQKE----K 401
Cdd:PRK04778 339 SYtlnESELESVRQLEKQLESLEKQYDEitERIaeQEIAY-SELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDeleaR 417
|
330 340
....*....|....*....|
gi 219521893 402 EQLQEEKQELLEYMRKLEAR 421
Cdd:PRK04778 418 EKLERYRNKLHEIKRYLEKS 437
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
143-441 |
1.49e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 143 ELRsRVQELERALATARQEHTELMEQYKGISRSHgEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLR 222
Cdd:PTZ00121 1192 ELR-KAEDARKAEAARKAEEERKAEEARKAEDAK-KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQ 1269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 223 DTVKALTREQEKLLGQLKEVQADKEQSEAE----LEPLK---EQLRGAQEL---AASSQQKATLLGE--ELASAAAARDR 290
Cdd:PTZ00121 1270 AAIKAEEARKADELKKAEEKKKADEAKKAEekkkADEAKkkaEEAKKADEAkkkAEEAKKKADAAKKkaEEAKKAAEAAK 1349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 291 TIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELA 370
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE 1429
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219521893 371 REKDSSLVQLSESKRELTELRSalrvlQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEA 441
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKK-----KAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEA 1495
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
112-411 |
1.60e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.95 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 112 KATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARqEHTELME----QYKGISRSHGEITEERDILS 187
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAAS-DHLNLVQtalrQQEKIERYQADLEELEERLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 188 RQQgdhvaRILELEDDIQTISE-KVLTKEVELDRLR----DTVKALTREQEKLLGQLKEVQA-DKEQSEAELEPLkeQLR 261
Cdd:PRK04863 366 EQN-----EVVEEADEQQEENEaRAEAAEEEVDELKsqlaDYQQALDVQQTRAIQYQQAVQAlERAKQLCGLPDL--TAD 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 262 GAQELAASSQQKATLLGEELASAAaaRDRTIAELHRSRLEVA-EVNGRLAelGLHLKEEKCQWSKERAGLLQSVEAEKDK 340
Cdd:PRK04863 439 NAEDWLEEFQAKEQEATEELLSLE--QKLSVAQAAHSQFEQAyQLVRKIA--GEVSRSEAWDVARELLRRLREQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 341 ILKLSAEILRLEKAVQEERTQNQVFKT----------------ELAREKDSSLVQLSESKRELTELRSALRvlqKEKEQL 404
Cdd:PRK04863 515 LQQLRMRLSELEQRLRQQQRAERLLAEfckrlgknlddedeleQLQEELEARLESLSESVSEARERRMALR---QQLEQL 591
|
....*..
gi 219521893 405 QEEKQEL 411
Cdd:PRK04863 592 QARIQRL 598
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
116-429 |
1.62e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.72 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQ-----LEGQVTELRSRVQELERALATARQEHTELMEQYKGISRshgEITEERDILSRQQ 190
Cdd:pfam15921 243 VEDQLEALKSESQNKIELLLQqhqdrIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE---QARNQNSMYMRQL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 191 GDHVARILEL-----------EDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQ 259
Cdd:pfam15921 320 SDLESTVSQLrselreakrmyEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQ 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 260 LRgaqelaassqqkatLLGEELASAAAARDRTIAELHRSRLEVAevngRLAELGLHLKEEkCQWSKERAglLQSVEAEKD 339
Cdd:pfam15921 400 NK--------------RLWDRDTGNSITIDHLRRELDDRNMEVQ----RLEALLKAMKSE-CQGQMERQ--MAAIQGKNE 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 340 KILKLSAEILRLE------KAVQEERTQNQVFKTELAREKDSSLVQLSESKR-------ELTELRSALRVLQKEKEQLQE 406
Cdd:pfam15921 459 SLEKVSSLTAQLEstkemlRKVVEELTAKKMTLESSERTVSDLTASLQEKERaieatnaEITKLRSRVDLKLQELQHLKN 538
|
330 340
....*....|....*....|....
gi 219521893 407 EKQELLEYMRKLEA-RLEKVADEK 429
Cdd:pfam15921 539 EGDHLRNVQTECEAlKLQMAEKDK 562
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
185-429 |
1.66e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 185 ILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQ 264
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 265 ELAASSQQKATLLGEELASAAAARDRtiaeLHRSRLEVAEVNGRLAELGLHLKEEKcqwsKERAGLLQSVEAEKDKILKL 344
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAER----LAEEELELEEALLAEEEEERELAEAE----EERLEEELEEEALEEQLEAE 733
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 345 SAEILRLEKAVQEERTqnqvfktELAREKDSSLVQLSESKRELTELRSALRVL--------------QKEKEQLQEEKQE 410
Cdd:COG1196 734 REELLEELLEEEELLE-------EEALEELPEPPDLEELERELERLEREIEALgpvnllaieeyeelEERYDFLSEQRED 806
|
250
....*....|....*....
gi 219521893 411 LLEYMRKLEARLEKVADEK 429
Cdd:COG1196 807 LEEARETLEEAIEEIDRET 825
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
199-428 |
1.82e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 199 ELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEaeleplkEQLRGAQELAASSQQKATLLG 278
Cdd:TIGR00618 191 SLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH-------AYLTQKREAQEEQLKKQQLLK 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 279 EELASAAAARDRTIA-ELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGlLQSVEAEKDKILKLSAEILRLEKAVQE 357
Cdd:TIGR00618 264 QLRARIEELRAQEAVlEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTE-LQSKMRSRAKLLMKRAAHVKQQSSIEE 342
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219521893 358 ERTQNQVFKTE---LAREKDSSLVQLSESKRElTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADE 428
Cdd:TIGR00618 343 QRRLLQTLHSQeihIRDAHEVATSIREISCQQ-HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTR 415
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
116-251 |
1.84e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQ----------------VTELRSRVQELERALATARQEHTE-------LMEQYKG- 171
Cdd:COG3206 224 LESQLAEARAELAEAEARLAALRAQlgsgpdalpellqspvIQQLRAQLAELEAELAELSARYTPnhpdviaLRAQIAAl 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 172 -------ISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKvltkEVELDRLRDTVKALTREQEKLLGQLKEVQA 244
Cdd:COG3206 304 raqlqqeAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL----EAELRRLEREVEVARELYESLLQRLEEARL 379
|
....*..
gi 219521893 245 DKEQSEA 251
Cdd:COG3206 380 AEALTVG 386
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
119-373 |
1.89e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.34 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 119 QLDESQQERNDLMQLKLQLEgqvtelRSRVQELERaLATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARIL 198
Cdd:pfam17380 354 RQEERKRELERIRQEEIAME------ISRMRELER-LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 199 ELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEklLGQLKEVQADKEQSEAELEPLKEQLRGAQElaassqQKATLLG 278
Cdd:pfam17380 427 AEQEEARQREVRRLEEERAREMERVRLEEQERQQQ--VERLRQQEEERKRKKLELEKEKRDRKRAEE------QRRKILE 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 279 EELasaaAARDRTIAELHRSRlEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEK--DKILKLSAEILRLEKAVQ 356
Cdd:pfam17380 499 KEL----EERKQAMIEEERKR-KLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRiqEQMRKATEERSRLEAMER 573
|
250
....*....|....*..
gi 219521893 357 EERTQNQVFKTELAREK 373
Cdd:pfam17380 574 EREMMRQIVESEKARAE 590
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
116-416 |
2.11e-04 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 44.29 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELerALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVA 195
Cdd:COG4192 39 LSNQIRYILDDSLPKLQASLKLEENSNELVAALPEF--AAATNTTERSQLRNQLNTQLADIEELLAELEQLTQDAGDLRA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 196 RILELEDDIQTISeKVLTKEVELDR---------------LRDTVKALTREQEKLLGQLKEVQADKEQSEAELeplkEQL 260
Cdd:COG4192 117 AVADLRNLLQQLD-SLLTQRIALRRrlqelleqinwlhqdFNSELTPLLQEASWQQTRLLDSVETTESLRNLQ----NEL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 261 RGAQELAASSQQKATLLGEelasAAAARD-RTIAELHRSRLE-VAEVNGRLAELGLHlkeekcqwskeragllqSVEAEK 338
Cdd:COG4192 192 QLLLRLLAIENQIVSLLRE----VAAARDqADVDNLFDRLQYlKDELDRNLQALKNY-----------------PSTITL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 339 DKILKLSAEILRLEKAVQEERTQNQVFktelarekDSSLVQLSESKRE-LTELRSALRVL-QKEKEQLQEEKQELLEYMR 416
Cdd:COG4192 251 RQLIDELLAIGSGEGGLPSLRRDELAA--------QATLEALAEENNSiLEQLRTQISGLvGNSREQLVALNQETAQLVQ 322
|
|
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
238-420 |
2.14e-04 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 42.68 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 238 QLKEVQADKEQSEAELEPLKEQLRgaqelaassqqkatllgeELASAAAARDRTIAELHrsrlevAEVNGRLAELglhlk 317
Cdd:pfam06818 18 QLKDSQAEVTQKLNEIVALRAQLR------------------ELRAKLEEKEEQIQELE------DSLRSKTLEL----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 318 eEKCQwsKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTE--LAREKDSSLVQLSESKRELTELRSALR 395
Cdd:pfam06818 69 -EVCE--NELQRKKNEAELLREKVGKLEEEVSGLREALSDVSPSGYESVYEsdEAKEQRQEEADLGSLRREVERLRAELR 145
|
170 180 190
....*....|....*....|....*....|....*.
gi 219521893 396 VLQKEKEQL-----------QEEKQELLEYMRKLEA 420
Cdd:pfam06818 146 EERQRRERQassfeqerrtwQEEKEKVIRYQKQLQL 181
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
121-363 |
2.69e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 121 DESQQERNDLMQLKLQ---LEGQVTELRSRVQELERALATARQEHTELMEQykgISRSHGEITEERDILSRQQ---GDHV 194
Cdd:COG3883 16 PQIQAKQKELSELQAEleaAQAELDALQAELEELNEEYNELQAELEALQAE---IDKLQAEIAEAEAEIEERReelGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 195 ARILELEDDIQTISEKVLTKEVE--LDRLrDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQq 272
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSESFSdfLDRL-SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 273 katllgEELASAAAARDRTIAELhrsRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLE 352
Cdd:COG3883 171 ------AELEAQQAEQEALLAQL---SAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
250
....*....|.
gi 219521893 353 KAVQEERTQNQ 363
Cdd:COG3883 242 AAASAAGAGAA 252
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
117-288 |
2.90e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 117 QNQLDESQQERNDLMQLKLQLEGQVTELR-------SRVQELERALATARQEHTELME--QYKGISRSHGEITEERDILS 187
Cdd:COG3206 204 KNGLVDLSEEAKLLLQQLSELESQLAEARaelaeaeARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELS 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 188 RQQGDH-------VARILELEDDIQTISEKVLTK-EVELDRLRDTVKALTREQEKLLGQLKEVQadkeQSEAELEPLKEQ 259
Cdd:COG3206 284 ARYTPNhpdvialRAQIAALRAQLQQEAQRILASlEAELEALQAREASLQAQLAQLEARLAELP----ELEAELRRLERE 359
|
170 180
....*....|....*....|....*....
gi 219521893 260 LRGAQELAASSQQKAtllgEELASAAAAR 288
Cdd:COG3206 360 VEVARELYESLLQRL----EEARLAEALT 384
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
137-296 |
2.93e-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: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 137 LEGQVTELRSRVQELERALAtaRQEHTElmEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEV 216
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLR--QQQNAE--RLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 217 ELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQkATLLGEELASAAAARDRTIAELH 296
Cdd:COG3096 586 QLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLERERE-ATVERDELAARKQALESQIERLS 664
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
138-407 |
3.03e-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: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 138 EGQVTELRSRVQELERALATARQEHTELMEQYKgisrshgEITEERDILSRQQG--------DHVARILELEDDIQTISE 209
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQLD-------QLKEQLQLLNKLLPqanlladeTLADRLEELREELDAAQE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 210 K---VLTKEVELDRLRDTVKALTREQEkllgQLKEVQADKEQSEAELEPLKEQLRGAQELAassqQKATLLGEELASAAA 286
Cdd:COG3096 908 AqafIQQHGKALAQLEPLVAVLQSDPE----QFEQLQADYLQAKEQQRRLKQQIFALSEVV----QRRPHFSYEDAVGLL 979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 287 ARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKC-QWSKERAGLLQSVEAEKDKILKLSAEILRL--------EKAVQE 357
Cdd:COG3096 980 GENSDLNEKLRARLEQAEEARREAREQLRQAQAQYsQYNQVLASLKSSRDAKQQTLQELEQELEELgvqadaeaEERARI 1059
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 219521893 358 ERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEE 407
Cdd:COG3096 1060 RRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQ 1109
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
180-442 |
3.10e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.79 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 180 TEERDILSRQQGDHVARILELEDDIQT------------ISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKE 247
Cdd:COG5185 241 PESELEDLAQTSDKLEKLVEQNTDLRLeklgenaesskrLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 248 -QSEAELEPLK-EQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRL--EVAEVNGRLAELGLHLKEEKCQW 323
Cdd:COG5185 321 aEAEQELEESKrETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSseELDSFKDTIESTKESLDEIPQNQ 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 324 SKERAGLLQSVEaekDKILKLSAEILRLEKAVQEERTQNQVFKTEL-----------AREKDSSLVQLSESKREL-TELR 391
Cdd:COG5185 401 RGYAQEILATLE---DTLKAADRQIEELQRQIEQATSSNEEVSKLLneliselnkvmREADEESQSRLEEAYDEInRSVR 477
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 219521893 392 SALRVLQKEKEQLQEEKQELLEYMRKLEARLEK---VADEKWNEDATTEDEEAA 442
Cdd:COG5185 478 SKKEDLNEELTQIESRVSTLKATLEKLRAKLERqleGVRSKLDQVAESLKDFMR 531
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
119-429 |
3.20e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 119 QLDESQQERNDLMQLKLQLEGqvteLRSRVQELERaLATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARIL 198
Cdd:pfam12128 318 AKDRSELEALEDQHGAFLDAD----IETAAADQEQ-LPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDI 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 199 E-LEDDIQTISE-KVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAEL----------EPLKEQLRGAQEL 266
Cdd:pfam12128 393 AgIKDKLAKIREaRDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELklrlnqatatPELLLQLENFDER 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 267 ---AASSQQKATL----LGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGL-----------HLKEEKCQWSKERA 328
Cdd:pfam12128 473 ierAREEQEAANAeverLQSELRQARKRRDQASEALRQASRRLEERQSALDELELqlfpqagtllhFLRKEAPDWEQSIG 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 329 GLLQS------------VEAEKDKILKL-----------------SAEILRLEKAVQEERTQNQvfkTELAREKDSSLVQ 379
Cdd:pfam12128 553 KVISPellhrtdldpevWDGSVGGELNLygvkldlkridvpewaaSEEELRERLDKAEEALQSA---REKQAAAEEQLVQ 629
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219521893 380 LS----ESKRELTELRSA-------LRVLQKEKEQLQEEKQELL-EYMRKLEARLEKVADEK 429
Cdd:pfam12128 630 ANgeleKASREETFARTAlknarldLRRLFDEKQSEKDKKNKALaERKDSANERLNSLEAQL 691
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
116-412 |
3.69e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVA 195
Cdd:COG4372 50 LREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 196 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEaelepLKEQLRGAQELAASSQQKAT 275
Cdd:COG4372 130 QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA-----LDELLKEANRNAEKEEELAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 276 LLGEELASaaaARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAV 355
Cdd:COG4372 205 AEKLIESL---PRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIA 281
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 219521893 356 QEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELL 412
Cdd:COG4372 282 ALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAE 338
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
135-429 |
3.84e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 135 LQLEGQVTELRSRVQELERALATARQEHTELMEQYKGIS---RSHGEITEERDILSRqqgdhvaRILELEDDIQTIsEKV 211
Cdd:PRK03918 296 IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEekeERLEELKKKLKELEK-------RLEELEERHELY-EEA 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 212 LTKEVELDRLRDTVKALTreQEKLLGQLKEVQADKEQSEAELEPLKE----------QLRGAQELAASSQQKATLLGEEL 281
Cdd:PRK03918 368 KAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITArigelkkeikELKKAIEELKKAKGKCPVCGREL 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 282 ASAAAAR--DRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKER--------AGLLQSVEAE-------------- 337
Cdd:PRK03918 446 TEEHRKEllEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkelAEQLKELEEKlkkynleelekkae 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 338 -----KDKILKLSAEILRLEKAVQEERTQNQVfKTELAREKDSSLVQLSESKRELT--------ELRSALRVLQK----- 399
Cdd:PRK03918 526 eyeklKEKLIKLKGEIKSLKKELEKLEELKKK-LAELEKKLDELEEELAELLKELEelgfesveELEERLKELEPfyney 604
|
330 340 350
....*....|....*....|....*....|....*
gi 219521893 400 -----EKEQLQEEKQELLEYMRKLEARLEKVADEK 429
Cdd:PRK03918 605 lelkdAEKELEREEKELKKLEEELDKAFEELAETE 639
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
116-443 |
5.01e-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: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLmqLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVA 195
Cdd:TIGR02168 412 LEDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 196 RILELEDDIQtisekvltkevELDRLRDTVKALTREQEKL------LGQLKEVQADKEQS-EAELEP---------LKEQ 259
Cdd:TIGR02168 490 RLDSLERLQE-----------NLEGFSEGVKALLKNQSGLsgilgvLSELISVDEGYEAAiEAALGGrlqavvvenLNAA 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 260 LRGAQELAASSQQKATLLGEELASAAA--ARDRTIAELHRSRLEVAE------------VNGRLAEL--------GLHL- 316
Cdd:TIGR02168 559 KKAIAFLKQNELGRVTFLPLDSIKGTEiqGNDREILKNIEGFLGVAKdlvkfdpklrkaLSYLLGGVlvvddldnALELa 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 317 KEEKCQW-------------------SKERAGLLQSVEAEKD----KILKLSAEILRLEKAVQEERTQNQVFKTELA--- 370
Cdd:TIGR02168 639 KKLRPGYrivtldgdlvrpggvitggSAKTNSSILERRREIEeleeKIEELEEKIAELEKALAELRKELEELEEELEqlr 718
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219521893 371 REKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEAAV 443
Cdd:TIGR02168 719 KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQI 791
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
195-428 |
5.01e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 195 ARILELEDDIQTISEKVLTKEVELDRLRDTVKA-LTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQK 273
Cdd:pfam05557 9 ARLSQLQNEKKQMELEHKRARIELEKKASALKRqLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 274 ATLLGEELASAAAARD------RTIAELHRS----RLEVAEVNGRLAELGLHLKEEKCQWSkERAGLLQSVEAEKDKILK 343
Cdd:pfam05557 89 NKKLNEKESQLADAREvisclkNELSELRRQiqraELELQSTNSELEELQERLDLLKAKAS-EAEQLRQNLEKQQSSLAE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 344 LSAEILRLEKAVQEERTQNQVFKTELARekdssLVQLSESKRELTELR---SALRVLQKEKEQLQEEKQellEYMRKLEa 420
Cdd:pfam05557 168 AEQRIKELEFEIQSQEQDSEIVKNSKSE-----LARIPELEKELERLRehnKHLNENIENKLLLKEEVE---DLKRKLE- 238
|
....*...
gi 219521893 421 RLEKVADE 428
Cdd:pfam05557 239 REEKYREE 246
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
116-265 |
5.04e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALaTARQEHTELMEQYKGISRSHGEITEerdiLSRQQGDHVA 195
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFEL-KKENLEKEIDEKNKEIEELKQTQKS----LKKKQEEKQE 589
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 196 RILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQE 265
Cdd:TIGR04523 590 LIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRN 659
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
120-428 |
5.67e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 120 LDESQQERNDLMQLKLQLEGQVTELRSRVQ-ELERALAtARQEHTELMEQykgISRSHGEITEERDILSRQQGDHVARIL 198
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMKSECQgQMERQMA-AIQGKNESLEK---VSSLTAQLESTKEMLRKVVEELTAKKM 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 199 ELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSE------AELEPLKEQLRGAQELAASSQQ 272
Cdd:pfam15921 490 TLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDhlrnvqTECEALKLQMAEKDKVIEILRQ 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 273 K----ATLLGEELASAAAArdrtiaELHRSRLEvAEVNGRLAELGLH--LKEEKCQWSKERAGLLQSVEAEKDKILKLSA 346
Cdd:pfam15921 570 QienmTQLVGQHGRTAGAM------QVEKAQLE-KEINDRRLELQEFkiLKDKKDAKIRELEARVSDLELEKVKLVNAGS 642
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 347 EILRLEKAVQEERTQ--NQV--FKTELA-------------REKDSSL--------VQLSESKRELTELRSALRVLQ--- 398
Cdd:pfam15921 643 ERLRAVKDIKQERDQllNEVktSRNELNslsedyevlkrnfRNKSEEMetttnklkMQLKSAQSELEQTRNTLKSMEgsd 722
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 219521893 399 ---------------------------------------KEKEQLQEEKQELLEYMRKLEARLEKVADE 428
Cdd:pfam15921 723 ghamkvamgmqkqitakrgqidalqskiqfleeamtnanKEKHFLKEEKNKLSQELSTVATEKNKMAGE 791
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
117-444 |
6.11e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 117 QNQLDESQQERNDLMQLKLQLEGQVTELR---SRVQELERALATARQE---HTELmEQYKGISRSHGEITEERDILSRQQ 190
Cdd:TIGR00606 325 QRELEKLNKERRLLNQEKTELLVEQGRLQlqaDRHQEHIRARDSLIQSlatRLEL-DGFERGPFSERQIKNFHTLVIERQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 191 GDHVARILELEDDIQtisEKVLTKEVELDRLRDTVKALTREqekllgqlkeVQADKEQSEAELEPLKEQLRGAQELAASS 270
Cdd:TIGR00606 404 EDEAKTAAQLCADLQ---SKERLKQEQADEIRDEKKGLGRT----------IELKKEILEKKQEELKFVIKELQQLEGSS 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 271 QQkatLLGEELASAAAARDRTIAElhrsrlEVAEVNGRLAELgLHLKEEKCQWSKERAGLLQSVEaEKDKILKLSAEILR 350
Cdd:TIGR00606 471 DR---ILELDQELRKAERELSKAE------KNSLTETLKKEV-KSLQNEKADLDRKLRKLDQEME-QLNHHTTTRTQMEM 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 351 LEKAVQEERTQNQVFKTELAREKDSSL------VQLSES----KRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEA 420
Cdd:TIGR00606 540 LTKDKMDKDEQIRKIKSRHSDELTSLLgyfpnkKQLEDWlhskSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE 619
|
330 340
....*....|....*....|....
gi 219521893 421 RLEKVADeKWNEDATTEDEEAAVG 444
Cdd:TIGR00606 620 QLSSYED-KLFDVCGSQDEESDLE 642
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
129-440 |
6.79e-04 |
|
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: 42.85 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 129 DLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHgeiteERDILSR-QQGDHVARIL--------- 198
Cdd:pfam01576 682 ELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQF-----ERDLQARdEQGEEKRRQLvkqvrelea 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 199 ELEDDIQTISEKVLTK---EVELDRLRDTVKALTREQE-------KLLGQLKEVQADKEQS------------------- 249
Cdd:pfam01576 757 ELEDERKQRAQAVAAKkklELDLKELEAQIDAANKGREeavkqlkKLQAQMKDLQRELEEArasrdeilaqskesekklk 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 250 --EAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAElhRSRLEvaevnGRLAELGLHLKEEKCqwsker 327
Cdd:pfam01576 837 nlEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDE--KRRLE-----ARIAQLEEELEEEQS------ 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 328 agllqSVEAEKDKILKLSAEILRLEKAVQEERTQNQvfKTELAREKDSSlvQLSESKRELTELRSALRVLQKE------- 400
Cdd:pfam01576 904 -----NTELLNDRLRKSTLQVEQLTTELAAERSTSQ--KSESARQQLER--QNKELKAKLQEMEGTVKSKFKSsiaalea 974
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 219521893 401 -----KEQLQEEKQElleymRKLEARLEKVADEKWNEDATTEDEE 440
Cdd:pfam01576 975 kiaqlEEQLEQESRE-----RQAANKLVRRTEKKLKEVLLQVEDE 1014
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
115-424 |
7.18e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 115 VLQNQLDESQQERNDLMQLKLQLEGQVTELRS---RVQELERALATARQEHTELMEqykgiSRSHGEITEERDILSRQQG 191
Cdd:pfam05557 136 ELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFEIQSQEQDSEIVKN-----SKSELARIPELEKELERLR 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 192 DHVARILELEDDIQTISEKVLTKEVELDRL---RDTVKALTREQEKLLGQLKEVQaDKEQSEAELEPLKEQLRGAQElaa 268
Cdd:pfam05557 211 EHNKHLNENIENKLLLKEEVEDLKRKLEREekyREEAATLELEKEKLEQELQSWV-KLAQDTGLNLRSPEDLSRRIE--- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 269 SSQQKATLLGEE---LASAAAARDRTIAELhrsRLEVAEVNGRLAELGLHLKEEKCQ----------WSKERAGLLQSVE 335
Cdd:pfam05557 287 QLQQREIVLKEEnssLTSSARQLEKARREL---EQELAQYLKKIEDLNKKLKRHKALvrrlqrrvllLTKERDGYRAILE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 336 ------AEKDKILKLSAEILRLEKAVQEERTQNQVFKTELA---REKDSSLVQLSESKRELTELRS------------AL 394
Cdd:pfam05557 364 sydkelTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSvaeEELGGYKQQAQTLERELQALRQqesladpsyskeEV 443
|
330 340 350
....*....|....*....|....*....|
gi 219521893 395 RVLQKEKEQLQEEKQELLEYMRKLEARLEK 424
Cdd:pfam05557 444 DSLRRKLETLELERQRLREQKNELEMELER 473
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
199-441 |
7.38e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 199 ELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEV--QADKEQSE-----AELEPLKEQLRGAQELAASSQ 271
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELreEAQELREKrdelnEKVKELKEERDELNEKLNELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 272 QKATLLGEELASAAAARdRTIAELHRsrlEVAEVNGRLAELGLHLKEE-----KCQWSKERAGLLQSVEAEKDKILKLSA 346
Cdd:COG1340 92 EELDELRKELAELNKAG-GSIDKLRK---EIERLEWRQQTEVLSPEEEkelveKIKELEKELEKAKKALEKNEKLKELRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 347 EILRLEKAVQEERTQnqvfKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEE-----------KQELLEYM 415
Cdd:COG1340 168 ELKELRKEAEEIHKK----IKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKadelheeiielQKELRELR 243
|
250 260
....*....|....*....|....*.
gi 219521893 416 RKLEARLEKVADEKWNEDATTEDEEA 441
Cdd:COG1340 244 KELKKLRKKQRALKREKEKEELEEKA 269
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
283-444 |
8.94e-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: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 283 SAAAARDRTIAELHRSRLEVAEVNGRLAELglhlKEEKCQWSKER---AGLLQSVEAEKDkILKLSAEILRLEKAVQEER 359
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEAL----EAELDALQERRealQRLAEYSWDEID-VASAEREIAELEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 360 TQNQVFKtELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDE 439
Cdd:COG4913 682 ASSDDLA-ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
|
....*
gi 219521893 440 EAAVG 444
Cdd:COG4913 761 DAVER 765
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
135-442 |
1.05e-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: 42.08 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 135 LQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVLTK 214
Cdd:pfam01576 639 LSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRL 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 215 EVELDRLRDTVKALTREQEKlLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKATL--LGEELASAAAARDRTI 292
Cdd:pfam01576 719 EVNMQALKAQFERDLQARDE-QGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLkeLEAQIDAANKGREEAV 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 293 AELHRSRLEVAEVNGRLAELGLHLKEEkcqwskeragLLQSVEAEKdKILKLSAEILRLEK---AVQEERTQNQVFKTEL 369
Cdd:pfam01576 798 KQLKKLQAQMKDLQRELEEARASRDEI----------LAQSKESEK-KLKNLEAELLQLQEdlaASERARRQAQQERDEL 866
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219521893 370 AREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEAA 442
Cdd:pfam01576 867 ADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESA 939
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
190-443 |
1.07e-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: 42.27 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 190 QGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEkllgQLKEVQADKEQSEAELEPLKEQLRGAQELAAS 269
Cdd:pfam02463 140 QGGKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETE----NLAELIIDLEELKLQELKLKEQAKKALEYYQL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 270 SQQKATLLGEELASaaaardrtiaELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEIL 349
Cdd:pfam02463 216 KEKLELEEEYLLYL----------DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 350 RLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSAlrvLQKEKEQLQEEKQELLEYMRKLEARLEKVADEK 429
Cdd:pfam02463 286 EELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE---LKKEKEEIEELEKELKELEIKREAEEEEEEELE 362
|
250
....*....|....
gi 219521893 430 WNEDATTEDEEAAV 443
Cdd:pfam02463 363 KLQEKLEQLEEELL 376
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
118-435 |
1.18e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 118 NQLDESQQERNDLMQLK---LQLEGQVTELR---SRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQG 191
Cdd:COG4913 651 QRLAEYSWDEIDVASAEreiAELEAELERLDassDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 192 DHVARILELEDDIQTIS----EKVLTKEVELDRLRDTVKALTREQEKLlgqlkevQADKEQSEAELEPLKEQLRGAQELA 267
Cdd:COG4913 731 ELQDRLEAAEDLARLELrallEERFAAALGDAVERELRENLEERIDAL-------RARLNRAEEELERAMRAFNREWPAE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 268 ASsqqkatllgeELASAAAARDRTIAELHrsrlevaevngRLAELGLHLKEEKcqWskerAGLLQsvEAEKDKILKLSAE 347
Cdd:COG4913 804 TA----------DLDADLESLPEYLALLD-----------RLEEDGLPEYEER--F----KELLN--ENSIEFVADLLSK 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 348 ILRLEKAVQEERTQ-NQvfktELAREK---------DSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRK 417
Cdd:COG4913 855 LRRAIREIKERIDPlND----SLKRIPfgpgrylrlEARPRPDPEVREFRQELRAVTSGASLFDEELSEARFAALKRLIE 930
|
330
....*....|....*...
gi 219521893 418 LEARLEKVADEKWNEDAT 435
Cdd:COG4913 931 RLRSEEEESDRRWRARVL 948
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
122-226 |
1.43e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 122 ESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGI-SRSHGEITEERDILSRQqgdhvARILEL 200
Cdd:COG2433 403 HEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEArSEERREIRKDREISRLD-----REIERL 477
|
90 100
....*....|....*....|....*.
gi 219521893 201 EDDIQTISEKVLTKEVELDRLRDTVK 226
Cdd:COG2433 478 ERELEEERERIEELKRKLERLKELWK 503
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
220-413 |
1.53e-03 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 39.92 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 220 RLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPlkeqlrGAQELAASSQQKATLLGEELAsaaaardrtiaELHRSR 299
Cdd:pfam08614 11 RLLDRTALLEAENAKLQSEPESVLPSTSSSKLSKAS------PQSASIQSLEQLLAQLREELA-----------ELYRSR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 300 levAEVNGRLAELG--LHLKEEKcqwSKERAGLLQSVEAEKDKilkLSAEILRLEKAVQEERTQNQVFKTELArekdssl 377
Cdd:pfam08614 74 ---GELAQRLVDLNeeLQELEKK---LREDERRLAALEAERAQ---LEEKLKDREEELREKRKLNQDLQDELV------- 137
|
170 180 190
....*....|....*....|....*....|....*.
gi 219521893 378 vqlseskreltELRSALRVLQKEKEQLQEEKQELLE 413
Cdd:pfam08614 138 -----------ALQLQLNMAEEKLRKLEKENRELVE 162
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
116-419 |
1.70e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.54 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELEralatarQEHTELMEQykgisrshgeITEERDILSRQQGDHVA 195
Cdd:TIGR04523 45 IKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILE-------QQIKDLNDK----------LKKNKDKINKLNSDLSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 196 RILELEDDIQTISekvlTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRgaqelaaSSQQKAT 275
Cdd:TIGR04523 108 INSEIKNDKEQKN----KLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKE-------ELENELN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 276 LLGEELASAAAARDRTIAELHRSRLEVA------EVNGRLAELGLHLKEEKCQWSKeragllqSVEAEKDKILKLSAEIL 349
Cdd:TIGR04523 177 LLEKEKLNIQKNIDKIKNKLLKLELLLSnlkkkiQKNKSLESQISELKKQNNQLKD-------NIEKKQQEINEKTTEIS 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219521893 350 RLEKAVQEERTQNQVFKTELaREKDSSLVQ----LSESKRELTELRSALRVLQKEKEQ--LQEEKQELLEYMRKLE 419
Cdd:TIGR04523 250 NTQTQLNQLKDEQNKIKKQL-SEKQKELEQnnkkIKELEKQLNQLKSEISDLNNQKEQdwNKELKSELKNQEKKLE 324
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
119-440 |
1.78e-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: 41.49 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 119 QLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDhVARIL 198
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTL-TQHIH 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 199 ELEDDIQTISEK--VLTKEVE-LDRLRDTVKALTREQEKLLGQLkevQADKEQSEAELEPLkEQLRGAQELAASSQQKAT 275
Cdd:TIGR00618 383 TLQQQKTTLTQKlqSLCKELDiLQREQATIDTRTSAFRDLQGQL---AHAKKQQELQQRYA-ELCAAAITCTAQCEKLEK 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 276 LLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKC-------------QWSKERAGLLQSVEAEKDKIL 342
Cdd:TIGR00618 459 IHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCplcgscihpnparQDIDNPGPLTRRMQRGEQTYA 538
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 343 KLSAEILRLEKAVQEERTQNQVFKTE--------------------------------------LAREKDSSLVQLSESK 384
Cdd:TIGR00618 539 QLETSEEDVYHQLTSERKQRASLKEQmqeiqqsfsiltqcdnrskedipnlqnitvrlqdltekLSEAEDMLACEQHALL 618
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 219521893 385 RELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNedATTEDEE 440
Cdd:TIGR00618 619 RKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHAL--SIRVLPK 672
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
116-442 |
1.99e-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: 41.31 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVA 195
Cdd:pfam01576 192 LEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 196 RILELEDDIQtiSEKVLTKEVELDR--LRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLK----EQLRGAQELAAS 269
Cdd:pfam01576 272 QISELQEDLE--SERAARNKAEKQRrdLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKkaleEETRSHEAQLQE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 270 SQQKATLLGEELASAAAARDRTIAELHRSRLEvaevngrlaelglhLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEIL 349
Cdd:pfam01576 350 MRQKHTQALEELTEQLEQAKRNKANLEKAKQA--------------LESENAELQAELRTLQQAKQDSEHKRKKLEGQLQ 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 350 RLE-KAVQEERTQNQ----VFKTELAREKDSSLVQLSESK--RELTELRSALRVLQKEKEQLQEEKQELLeymrKLEARL 422
Cdd:pfam01576 416 ELQaRLSESERQRAElaekLSKLQSELESVSSLLNEAEGKniKLSKDVSSLESQLQDTQELLQEETRQKL----NLSTRL 491
|
330 340
....*....|....*....|
gi 219521893 423 EKVADEKWNEDATTEDEEAA 442
Cdd:pfam01576 492 RQLEDERNSLQEQLEEEEEA 511
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
195-303 |
2.14e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.48 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 195 ARILELEDDIQTISEKVLTKEVELDRLRDTVKALT---REQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAAS-- 269
Cdd:pfam00529 58 AALDSAEAQLAKAQAQVARLQAELDRLQALESELAisrQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIgg 137
|
90 100 110
....*....|....*....|....*....|....*
gi 219521893 270 -SQQKATLLGEELASAAAARDRTIAELHRSRLEVA 303
Cdd:pfam00529 138 iSRESLVTAGALVAQAQANLLATVAQLDQIYVQIT 172
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
178-441 |
2.21e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 178 EITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLK 257
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 258 EQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAE 337
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 338 KDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKE--QLQEEKQELLEYM 415
Cdd:COG4372 202 LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAilVEKDTEEEELEIA 281
|
250 260
....*....|....*....|....*.
gi 219521893 416 RKLEARLEKVADEKWNEDATTEDEEA 441
Cdd:COG4372 282 ALELEALEEAALELKLLALLLNLAAL 307
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
225-460 |
2.24e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 225 VKALTREQEKLLGQLKEVQADKEQSEaelepLKEQLRGAQELAASSQQKATLLGEELASAAAARDR---TIAELHRSRLE 301
Cdd:PRK02224 178 VERVLSDQRGSLDQLKAQIEEKEEKD-----LHERLNGLESELAELDEEIERYEEQREQARETRDEadeVLEEHEERREE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 302 VAEVNGRLAElglhLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRL----------EKAVQEERTQNQVFKTELAR 371
Cdd:PRK02224 253 LETLEAEIED----LRETIAETEREREELAEEVRDLRERLEELEEERDDLlaeaglddadAEAVEARREELEDRDEELRD 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 372 EKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEAAVGLScPAAL 451
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA-PVDL 407
|
....*....
gi 219521893 452 TDSEDESPE 460
Cdd:PRK02224 408 GNAEDFLEE 416
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
116-261 |
2.41e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTEL---MEQYKGIS---RSHGE-------ITEE 182
Cdd:PHA02562 218 KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIkskIEQFQKVIkmyEKGGVcptctqqISEG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 183 RDILS--RQQGDHVARILELEDDIQtisEKVLTKEVELDRLRDTVKALTREQEKLLGQL-------KEVQADKEQSEA-- 251
Cdd:PHA02562 298 PDRITkiKDKLKELQHSLEKLDTAI---DELEEIMDEFNEQSKKLLELKNKISTNKQSLitlvdkaKKVKAAIEELQAef 374
|
170
....*....|....*
gi 219521893 252 -----ELEPLKEQLR 261
Cdd:PHA02562 375 vdnaeELAKLQDELD 389
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
114-315 |
2.46e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 40.48 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 114 TVLQNQLDESQqerNDLMQLKLQLEGQVTElRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDh 193
Cdd:pfam00529 54 TDYQAALDSAE---AQLAKAQAQVARLQAE-LDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 194 vARILELEDDIqtISEKVltkeVELDRLRDTVKAltrEQEKLLGQLKEVQADKEQSEAELEplkeqlrgaqelaasSQQK 273
Cdd:pfam00529 129 -RRVLAPIGGI--SRESL----VTAGALVAQAQA---NLLATVAQLDQIYVQITQSAAENQ---------------AEVR 183
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 219521893 274 ATLLGEELASAAAARDRTIAELHRSRLEV-AEVNGRLAELGLH 315
Cdd:pfam00529 184 SELSGAQLQIAEAEAELKLAKLDLERTEIrAPVDGTVAFLSVT 226
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
116-427 |
2.46e-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: 40.93 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 116 LQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVA 195
Cdd:pfam01576 754 LEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEK 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 196 RILELEDDIQTISEKVLTKEveldRLRDTVKALTRE-QEKLLGQLKE---VQADKEQSEAELEPLKEQLRGAQ---ELAA 268
Cdd:pfam01576 834 KLKNLEAELLQLQEDLAASE----RARRQAQQERDElADEIASGASGksaLQDEKRRLEARIAQLEEELEEEQsntELLN 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 269 SSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNgrlAELGLHLKEEKcqwskeragllQSVEAE-KDKILKLSAE 347
Cdd:pfam01576 910 DRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQN---KELKAKLQEME-----------GTVKSKfKSSIAALEAK 975
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 348 ILRLEKAVQEERTQNQVfKTELAREKDSSL----VQLSESKR-------ELTELRSALRVLQKEKEQLQEEKQELLEYMR 416
Cdd:pfam01576 976 IAQLEEQLEQESRERQA-ANKLVRRTEKKLkevlLQVEDERRhadqykdQAEKGNSRMKQLKRQLEEAEEEASRANAARR 1054
|
330
....*....|.
gi 219521893 417 KLEARLEKVAD 427
Cdd:pfam01576 1055 KLQRELDDATE 1065
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
316-420 |
2.47e-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: 39.50 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 316 LKEEKCQwskeraglLQSVEAEKDKILK-LSAEILRLEKAVQEERTQNQVFKTELAR-EKDsslvqlsesKRELTELRSA 393
Cdd:pfam13851 31 LKEEIAE--------LKKKEERNEKLMSeIQQENKRLTEPLQKAQEEVEELRKQLENyEKD---------KQSLKNLKAR 93
|
90 100
....*....|....*....|....*..
gi 219521893 394 LRVLQKEKEQLQEEKQELLEYMRKLEA 420
Cdd:pfam13851 94 LKVLEKELKDLKWEHEVLEQRFEKVER 120
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
194-426 |
2.52e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 194 VARILELeDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRG-AQELAASSQQ 272
Cdd:PRK03918 151 VRQILGL-DDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPElREELEKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 273 KATLlgEELASaaaardrtiaELHRSRLEVAEVNGRLAELglhlkEEKCQWSKERaglLQSVEAEKDKILKLSAEILRLE 352
Cdd:PRK03918 230 VKEL--EELKE----------EIEELEKELESLEGSKRKL-----EEKIRELEER---IEELKKEIEELEEKVKELKELK 289
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219521893 353 KAVQEERtqnqvfktELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVA 426
Cdd:PRK03918 290 EKAEEYI--------KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLE 355
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
183-406 |
2.76e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.44 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 183 RDILsrqqgDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEV-QAD-KEQSEAELEPLKEQL 260
Cdd:COG0497 144 RELL-----DAFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELeAAAlQPGEEEELEEERRRL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 261 RGAQELAASSQQKATLLGEELASAAAARDRTIAELHR-SRL--EVAEVNGRLAELGLHLKEEKCQWSKERAGL------L 331
Cdd:COG0497 219 SNAEKLREALQEALEALSGGEGGALDLLGQALRALERlAEYdpSLAELAERLESALIELEEAASELRRYLDSLefdperL 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 332 QSVEAEKDKILKLS-------AEILRLEKAVQEERTQNQVFKT---ELAREKDSSLVQLSESKRELTELRS-ALRVLQKE 400
Cdd:COG0497 299 EEVEERLALLRRLArkygvtvEELLAYAEELRAELAELENSDErleELEAELAEAEAELLEAAEKLSAARKkAAKKLEKA 378
|
....*..
gi 219521893 401 -KEQLQE 406
Cdd:COG0497 379 vTAELAD 385
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
140-441 |
2.78e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 140 QVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEIT----EERDILSRQQGDHVARILELEDDIQTISEKVLTKE 215
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAikaeEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 216 VELDRLRDTVKALTREQEKLLGQLKEvQADKEQSEAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAEL 295
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKK-KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 296 HRSRLEV---AEVNGRLAElglHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILR----LEKAVQEERTQNQVFKTE 368
Cdd:PTZ00121 1390 KKKADEAkkkAEEDKKKAD---ELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKkadeAKKKAEEAKKAEEAKKKA 1466
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 219521893 369 LAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQElleymrKLEARLEKVADEKWNEDATTEDEEA 441
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA------KKKADEAKKAEEAKKADEAKKAEEA 1533
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
107-426 |
2.91e-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: 40.49 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 107 LLVVPKATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATA-----RQEHTEL-MEQYKGISRSHGEIT 180
Cdd:pfam05557 196 LARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAatlelEKEKLEQeLQSWVKLAQDTGLNL 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 181 EERDILSRqqgdhvaRILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQL 260
Cdd:pfam05557 276 RSPEDLSR-------RIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRV 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 261 RGA---------------QELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSK 325
Cdd:pfam05557 349 LLLtkerdgyrailesydKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALR 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 326 ERAGLL-QSVEAEKDKILKLSAEILRLEkaVQEERTQNQVFKTELARE--------KDSSLVQLSESKRELtelrsALRV 396
Cdd:pfam05557 429 QQESLAdPSYSKEEVDSLRRKLETLELE--RQRLREQKNELEMELERRclqgdydpKKTKVLHLSMNPAAE-----AYQQ 501
|
330 340 350
....*....|....*....|....*....|
gi 219521893 397 LQKEKEQLQEEKQELLEYMRKLEARLEKVA 426
Cdd:pfam05557 502 RKNQLEKLQAEIERLKRLLKKLEDDLEQVL 531
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
129-260 |
3.03e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.00 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 129 DLMQLKLQLEGQVTELRSR--------------VQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQqgdhV 194
Cdd:smart00787 113 LLMDKQFQLVKTFARLEAKkmwyewrmklleglKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEE----L 188
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219521893 195 ARILELEDDIQTIsekvltKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQL 260
Cdd:smart00787 189 RQLKQLEDELEDC------DPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKK 248
|
|
| ADIP |
pfam11559 |
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ... |
335-425 |
3.13e-03 |
|
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.
Pssm-ID: 463295 [Multi-domain] Cd Length: 151 Bit Score: 38.45 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 335 EAEKDKILKLSAEILRLEKAVQEERTQNQvfktELAREKDSSLVQLSESKRELTELRSALR----VLQKEKEQLQEEKQE 410
Cdd:pfam11559 55 ESLNETIRTLEAEIERLQSKIERLKTQLE----DLERELALLQAKERQLEKKLKTLEQKLKnekeELQRLKNALQQIKTQ 130
|
90
....*....|....*
gi 219521893 411 LLEYMRKLEARLEKV 425
Cdd:pfam11559 131 FAHEVKKRDREIEKL 145
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
135-313 |
5.16e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 135 LQLEGQVTELRSRVQELERALATARQEHTELMEqyKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVLTK 214
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRA--VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 215 EVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAE 294
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
170
....*....|....*....
gi 219521893 295 LHRsrlEVAEVNGRLAELG 313
Cdd:COG1196 765 LER---ELERLEREIEALG 780
|
|
| Zn-C2H2_TAX1BP1_rpt2 |
cd21970 |
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar ... |
569-595 |
6.05e-03 |
|
second C2H2-type zinc binding domain found in tax1-binding protein 1 (TAX1BP1) and similar proteins; TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. It inhibits TNF-induced apoptosis by mediating the TNFAIP3 anti-apoptotic activity. It may also play a role in the pro-inflammatory cytokine IL-1 signaling cascade. TAX1BP1 is degraded by caspase-3-like family proteins upon TNF-induced apoptosis. TAX1BP1 contains two C2H2-type zinc binding domains; this model corresponds to the second one.
Pssm-ID: 412016 Cd Length: 27 Bit Score: 34.45 E-value: 6.05e-03
10 20
....*....|....*....|....*..
gi 219521893 569 KECPICKERFPAESDKDALEDHMDGHF 595
Cdd:cd21970 1 KVCPMCSEQFPPDCDQQVFERHVQTHF 27
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
375-429 |
6.47e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 38.94 E-value: 6.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 219521893 375 SSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEK 429
Cdd:COG4026 125 QNIPEYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREEN 179
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
120-432 |
6.79e-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: 39.57 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 120 LDESQQERNDLMQLKLQLEgQVTELRSRVQELERALATARQEhteLMEQYKGisrshgeiteERDILSRQQGDHVARILE 199
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLD-QYTQLALMEFAKKKSLHGKAEL---LTLRSQL----------LTLCTPCMPDTYHERKQV 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 200 LEDDIQTISEkvltkevELDRLRDTVKALTREQEKLLGQLKEVQADKEQ---------SEAELEPLKEQL---------- 260
Cdd:TIGR00618 224 LEKELKHLRE-------ALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLrarieelraQEAVLEETQERInrarkaapla 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 261 ----------RGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVA-----EVNGRLAELGLHLKEEKCQWSK 325
Cdd:TIGR00618 297 ahikavtqieQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhsqeIHIRDAHEVATSIREISCQQHT 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 326 ERAGLLQSVE-----AEKDKILKLSAEILRLEKAVQEERTQNQ--------VFKTELAREKDSSLVQLSESKRELTELRS 392
Cdd:TIGR00618 377 LTQHIHTLQQqkttlTQKLQSLCKELDILQREQATIDTRTSAFrdlqgqlaHAKKQQELQQRYAELCAAAITCTAQCEKL 456
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 219521893 393 ALRVLQKEKEQLQEEKQEL--LEYMRKLEARLEKVADEKWNE 432
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQLqtKEQIHLQETRKKAVVLARLLE 498
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
97-298 |
7.30e-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: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 97 LEEADGGSDILlvvpkaTVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSH 176
Cdd:COG4913 677 LERLDASSDDL------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 177 GE-----------ITEERDILSRQQGDHVARILELEDDIQTISEKVLTK-EVELDRLRDTVKALtREQEKLLGQLKEVqa 244
Cdd:COG4913 751 LEerfaaalgdavERELRENLEERIDALRARLNRAEEELERAMRAFNREwPAETADLDADLESL-PEYLALLDRLEED-- 827
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 219521893 245 dkeqseaELEPLKEQLRGAQElAASSQQKATLLGEELASAAAARDRtIAELHRS 298
Cdd:COG4913 828 -------GLPEYEERFKELLN-ENSIEFVADLLSKLRRAIREIKER-IDPLNDS 872
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
93-443 |
7.33e-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: 39.57 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 93 ELVTLEEADGGSDILLVVPKATVLQNQLDESQQERNDLMQLKLQLEG---QVTELRSRVQELERALATARQEHTELMEQY 169
Cdd:TIGR00618 479 EQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPltrRMQRGEQTYAQLETSEEDVYHQLTSERKQR 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 170 KGISRSHGEITEERDILSRQqgdhvarileleddIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQS 249
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQC--------------DNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 250 EAELEPLKEQLRGAQELAassQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAG 329
Cdd:TIGR00618 625 QDLQDVRLHLQQCSQELA---LKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQ 701
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 330 LLQSVEAEKDKILKLSAEILRLEKAV--------QEERTQNQVFKT--ELAREKDSSLVQLSESKRE--------LTELR 391
Cdd:TIGR00618 702 CQTLLRELETHIEEYDREFNEIENASsslgsdlaAREDALNQSLKElmHQARTVLKARTEAHFNNNEevtaalqtGAELS 781
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 219521893 392 SALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEAAV 443
Cdd:TIGR00618 782 HLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQF 833
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
224-406 |
7.40e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.51 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 224 TVKALTREQEkLLGQLKEVQADKEQSEAELEPLKEQLRGAQ-ELAASSQQKATLLGEELASAAAAR-----DRTIAELHR 297
Cdd:PRK11281 61 VQQDLEQTLA-LLDKIDRQKEETEQLKQQLAQAPAKLRQAQaELEALKDDNDEETRETLSTLSLRQlesrlAQTLDQLQN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 298 SRLEVAEVNGRLAelGLHLKEEKCQ--------WSKERAGLLQSVEAEK-----DKILKLSAEILRLEkavqeerTQNQV 364
Cdd:PRK11281 140 AQNDLAEYNSQLV--SLQTQPERAQaalyansqRLQQIRNLLKGGKVGGkalrpSQRVLLQAEQALLN-------AQNDL 210
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 219521893 365 FKTELarEKDSSLVQLSESKRELTELRSALrvLQKEKEQLQE 406
Cdd:PRK11281 211 QRKSL--EGNTQLQDLLQKQRDYLTARIQR--LEHQLQLLQE 248
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
214-374 |
7.48e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 7.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 214 KEVELDRLRDTVKA-----------LTREQEKLLG-QLKEVQADKEQSEAELEPLKEQLRgaqelaassqqkatllgeel 281
Cdd:COG2433 357 KKVPPDVDRDEVKArvirglsieeaLEELIEKELPeEEPEAEREKEHEERELTEEEEEIR-------------------- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 282 asaaaARDRTIAEL--HRSRL--EVAEVNGRLAELGLHLKEEKcqwSKERAgllqsvEAEKD-KILKLSAEILRLEKAVQ 356
Cdd:COG2433 417 -----RLEEQVERLeaEVEELeaELEEKDERIERLERELSEAR---SEERR------EIRKDrEISRLDREIERLERELE 482
|
170
....*....|....*...
gi 219521893 357 EERTQNQVFKTELAREKD 374
Cdd:COG2433 483 EERERIEELKRKLERLKE 500
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
124-265 |
7.67e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 124 QQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDilsrqqgDHVARILELEDD 203
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERD-------ELEAQLRELERK 904
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219521893 204 IQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQsEAELEPLKEQLRGAQE 265
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAELQRVEE 965
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
289-441 |
8.16e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 38.73 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 289 DRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFK-- 366
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEee 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219521893 367 -TELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEA 441
Cdd:COG4372 82 lEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
140-441 |
8.31e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 140 QVTELRSRVQELERALATARQEHTELmeqykgisrshgeiteerdilSRQQGDHVARILELEDDIQTISekvltkevelD 219
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEM---------------------ARELAELNEAESDLEQDYQAAS----------D 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 220 RLRDTVKALtREQEKLlgqlKEVQADKEQSEAELEPLKEQLRGAQELAASSQQKATLLGEELASAAA------------- 286
Cdd:PRK04863 336 HLNLVQTAL-RQQEKI----ERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSqladyqqaldvqq 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 287 -----------ARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEkcqwSKERAGL---LQSVEAEKDKILKLSAEILRLE 352
Cdd:PRK04863 411 traiqyqqavqALERAKQLCGLPDLTADNAEDWLEEFQAKEQEA----TEELLSLeqkLSVAQAAHSQFEQAYQLVRKIA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 353 KAVQEERTQNQVFKTELAREKDSSLVQ--------LSESKRELTELRSALRVLQ--KEKEQLQEEKQELLE-YMRKLEAR 421
Cdd:PRK04863 487 GEVSRSEAWDVARELLRRLREQRHLAEqlqqlrmrLSELEQRLRQQQRAERLLAefCKRLGKNLDDEDELEqLQEELEAR 566
|
330 340
....*....|....*....|
gi 219521893 422 LEKVADEKWNEDATTEDEEA 441
Cdd:PRK04863 567 LESLSESVSEARERRMALRQ 586
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
330-429 |
8.49e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 37.17 E-value: 8.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 330 LLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQ-LQEEK 408
Cdd:pfam03938 10 ILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQeLQKKQ 89
|
90 100
....*....|....*....|..
gi 219521893 409 QELLE-YMRKLEARLEKVADEK 429
Cdd:pfam03938 90 QELLQpIQDKINKAIKEVAKEK 111
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
127-266 |
8.80e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 38.46 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 127 RNDLMQ-LKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITE-ERDILSRQQGD---HVARILELE 201
Cdd:smart00787 138 RMKLLEgLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQlEDELEDCDPTEldrAKEKLKKLL 217
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 219521893 202 DDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQ----SEAELEPLKEQLRGAQEL 266
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQcrgfTFKEIEKLKEQLKLLQSL 286
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
120-407 |
9.08e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 39.12 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 120 LDESQQERNDLMQLKLQLEGQV-TELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARIL 198
Cdd:pfam15964 355 LIQCEQLKSELERQKERLEKELaSQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 199 ELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLK-EVQADKEQSEAELEPLKEQLRGAQELAASSQQKATLL 277
Cdd:pfam15964 435 EAQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRtKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARA 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 278 GEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKA--- 354
Cdd:pfam15964 515 REECLKLTELLGESEHQLHLTRLEKESIQQSFSNEAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTfia 594
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 219521893 355 -VQEERTQNQVFKTELAREKDSSLVQLSESKRELTElrsALRVLQKEKEQLQEE 407
Cdd:pfam15964 595 kLKEECCTLAKKLEEITQKSRSEVEQLSQEKEYLQD---RLEKLQKRNEELEEQ 645
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
238-423 |
9.91e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 38.52 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 238 QLKEVQAD---KEQSeaelepLKEQlrgaqelaasSQQKATLLGE----ELASAAAARdrtiaELHRSRLEVAEVNGRLA 310
Cdd:PRK11637 48 QLKSIQQDiaaKEKS------VRQQ----------QQQRASLLAQlkkqEEAISQASR-----KLRETQNTLNQLNKQID 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521893 311 ELGLHLKEEKCQWSKERAGLLQSVEAE----KDKILKLsaeILRLEKAVQEERTQ------NQvfktelAREKdsSLVQL 380
Cdd:PRK11637 107 ELNASIAKLEQQQAAQERLLAAQLDAAfrqgEHTGLQL---ILSGEESQRGERILayfgylNQ------ARQE--TIAEL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 219521893 381 SESKRELTELRSALrvlqkekEQLQEEKQELLEYMRKLEARLE 423
Cdd:PRK11637 176 KQTREELAAQKAEL-------EEKQSQQKTLLYEQQAQQQKLE 211
|
|
| |
