|
Name |
Accession |
Description |
Interval |
E-value |
| HD_SAS6_N |
cd10142 |
N-terminal head domain found in spindle assembly abnormal protein 6 and similar proteins; ... |
7-109 |
3.02e-46 |
|
N-terminal head domain found in spindle assembly abnormal protein 6 and similar proteins; Spindle assembly abnormal protein 6 (SAS6) is a central scaffolding component of the centrioles that ensures their 9-fold symmetry. It is required for centrosome biogenesis and duplication, and is required for both mother-centriole-dependent centriole duplication and deuterosome-dependent centriole amplification in multiciliated cells. It is also required for the recruitment of microcephaly protein STIL to the procentriole and for STIL-mediated centriole amplification. SAS6 is comprised of an N-terminal globular head domain, a centrally located coiled-coil domain, and a disordered C-terminus. These monomers homodimerize symmetrically, through two dimerization domains, the N-terminal globular head domains and long extended alpha-helical coiled-coil regions. These homodimers can self-assemble into a 9-fold symmetric cartwheel structure comprised of nine SAS6 homodimers associated via their head domains; the dimerized coiled-coil domains being the spokes, the central hub being the head domains. This model corresponds to the N-terminal head domain of SAS6, which is structurally related to other XRCC4-superfamily members, XRCC4, PAXX, XLF and CCDC61.
Pssm-ID: 408998 Cd Length: 137 Bit Score: 159.64 E-value: 3.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 7 EDLVIRLTDDTDPFFLYNLVISEEDFQSLKLQQGLLVDFLAFPQKFIDLLQQCMQEHAKETPRFLLQLLSSAtllENSPV 86
Cdd:cd10142 38 KELRVRLTDETDLFFLYTLELNEEDFQSLKEQQGLLVDFSAFPQKLIDLLELCIKEESKEPPKFLLVLVISS---DKGRA 114
|
90 100
....*....|....*....|...
gi 575771867 87 LLNVVETNPFKHLIHLSLKLLPG 109
Cdd:cd10142 115 TLEIVETNPFKHLTHLSLKFLPG 137
|
|
| SAS-6_N |
pfam16531 |
Centriolar protein SAS N-terminal; SAS-6_N is the N-terminal domain of the SAS-6 centriolar ... |
9-106 |
5.39e-28 |
|
Centriolar protein SAS N-terminal; SAS-6_N is the N-terminal domain of the SAS-6 centriolar protein, both in C.elegans and in humans. The N-terminal domain is the region through which the 9 rod-shaped homodimers that SAS-6 forms on oligomerization interact with each other. Proper functioning of the centriole requires this correct oligomerization.
Pssm-ID: 465163 Cd Length: 88 Bit Score: 107.28 E-value: 5.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 9 LVIRLTDDTDPFFLYNLVISEEDFQSLKLQQGLLVDFLAFPQKFIDLLQQCMQEhaketprfllQLLSSATLLENSPVLL 88
Cdd:pfam16531 1 LRIELTDDSDLFFLYILEIDEEDFESLKQEQNLLVDFEDFPQKLIKLLNNCIKE----------PNLLVFLIQDDGTATL 70
|
90
....*....|....*...
gi 575771867 89 NVVETNPFKHLIHLSLKL 106
Cdd:pfam16531 71 VFIENNEFKNLEHLSLDF 88
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
130-415 |
1.99e-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: 80.10 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 130 LSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEwashtasltnkhSQELTAEKEKALQTQVQCQQQHEQQKKELETLHQ 209
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKE------------LEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 210 R------NIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHIN 283
Cdd:TIGR02168 741 EveqleeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 284 QLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLM 363
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 575771867 364 GKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAgqflrakEQEVCRLQEQL 415
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGL-------EVRIDNLQERL 945
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
149-447 |
1.49e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 149 TLSEKMQELDK----LRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETLHQRnIHQLQSRLSELEA 224
Cdd:COG1196 217 ELKEELKELEAelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 225 ANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVL 304
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 305 RTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKE 384
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 575771867 385 EMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNE-KLITWLNKELNENQ 447
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGL 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
208-447 |
2.60e-12 |
|
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: 70.09 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 208 HQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQT 287
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 288 KVAVLEQEI------KDKDQLVL-RTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLK 360
Cdd:TIGR02168 317 QLEELEAQLeeleskLDELAEELaELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 361 TLMGKLK-LKNTVTI---QQEKLLAEKEEMLQK-ERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKL 435
Cdd:TIGR02168 397 SLNNEIErLEARLERledRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250
....*....|..
gi 575771867 436 ITWLNKELNENQ 447
Cdd:TIGR02168 477 LDAAERELAQLQ 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
132-435 |
3.28e-12 |
|
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: 69.70 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 132 LTRsLDDVTRQLHITQETL---SEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETL- 207
Cdd:TIGR02168 188 LDR-LEDILNELERQLKSLerqAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELe 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 208 -----HQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHI 282
Cdd:TIGR02168 267 ekleeLRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 283 NQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ------KVA-LEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKL 355
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQletlrsKVAqLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 356 Q-----GDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEE------ 424
Cdd:TIGR02168 427 LkkleeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENlegfse 506
|
330
....*....|..
gi 575771867 425 -SKQLLKNNEKL 435
Cdd:TIGR02168 507 gVKALLKNQSGL 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
201-455 |
2.37e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 201 KKELETL-HQRNIHQLQSRLSELEAANKELTERKykgdSTVRELKAKLAGVEEELQRAKQEVLSLRRENctldtecHEKE 279
Cdd:COG1196 219 KEELKELeAELLLLKLRELEAELEELEAELEELE----AELEELEAELAELEAELEELRLELEELELEL-------EEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 280 KHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEEngeknqiQLGKLEATIKSLSAELLKANEIIKKLQGDL 359
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE-------ELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 360 KTLMGKLKLKNTVTIQ-QEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITW 438
Cdd:COG1196 361 AEAEEALLEAEAELAEaEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250
....*....|....*..
gi 575771867 439 LNKELNENQLVRKQDTL 455
Cdd:COG1196 441 EEALEEAAEEEAELEEE 457
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
127-445 |
8.52e-11 |
|
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: 65.09 E-value: 8.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 127 EEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEwashtasltnkhsqELTAEKEKALQTQVQCQQQHEQQKKELEt 206
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE--------------REKAERYQALLKEKREYEGYELLKEKEA- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 207 lHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEvlslrrENCTLDTECHEKEKHINQLQ 286
Cdd:TIGR02169 235 -LERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE------EQLRVKEKIGELEAEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 287 TKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKL 366
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 367 KlknTVTIQQEKLLAEKEEM------LQKERKESQDAGQFLRAK-----------EQEVCRLQEQLETTVQKLEESKQLL 429
Cdd:TIGR02169 388 K---DYREKLEKLKREINELkreldrLQEELQRLSEELADLNAAiagieakinelEEEKEDKALEIKKQEWKLEQLAADL 464
|
330
....*....|....*.
gi 575771867 430 KNNEKLITWLNKELNE 445
Cdd:TIGR02169 465 SKYEQELYDLKEEYDR 480
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
213-452 |
9.63e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 9.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 213 HQLQSRLSELEAankELTERKYkgdstvRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVL 292
Cdd:COG1196 216 RELKEELKELEA---ELLLLKL------RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 293 EQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTV 372
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 373 TIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 452
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
126-398 |
2.08e-10 |
|
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: 63.92 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 126 KEEKLSLTRSLDDVTRQLHITQETLSEKM-------QELDKLRSEWASHTASLTNKHSQ-ELTAEKEKALQTQVQCQQQH 197
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRlevseleEEIEELQKELYALANEISRLEQQkQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 198 EQQKKELETLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHE 277
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 278 KEKHINQLQTKVAVLEQEIKDKDQLVLRTKeaFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQG 357
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 575771867 358 DLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAG 398
Cdd:TIGR02168 483 ELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILG 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
227-452 |
3.73e-10 |
|
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: 63.15 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 227 KELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENctldtecHEKEKHINQLQTKVAVLEQEIKDKDQLVLRT 306
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL-------EELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 307 KEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAEllkaneiIKKLQGDLKTlmgklkLKNTVTIQQEKLLAEKEEM 386
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ-------IEQLKEELKA------LREALDELRAELTLLNEEA 819
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575771867 387 LQKERKESQDAGQfLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 452
Cdd:TIGR02168 820 ANLRERLESLERR-IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
126-391 |
3.87e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 126 KEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQtqvqcqqqheqqkKELE 205
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL-------------EERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 206 TLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENctldtecHEKEKHINQL 285
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-------AEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 286 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGK 365
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260
....*....|....*....|....*.
gi 575771867 366 LKLKNTVTIQQEKLLAEKEEMLQKER 391
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAA 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
201-451 |
1.64e-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: 61.24 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 201 KKELETLHQR------NIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTE 274
Cdd:TIGR02169 687 KRELSSLQSElrrienRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 275 CHEKEKHINQLQTKVAVLEQEIKDkdqlvlrtkEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKK 354
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSH---------SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 355 LQGDLKTLMGKlklKNTVTIQQEKLLAEKEEMLQKERKesqdagqfLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEK 434
Cdd:TIGR02169 838 LQEQRIDLKEQ---IKSIEKEIENLNGKKEELEEELEE--------LEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
250
....*....|....*..
gi 575771867 435 LITWLNKELNENQLVRK 451
Cdd:TIGR02169 907 ELEAQIEKKRKRLSELK 923
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
209-452 |
3.83e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 3.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 209 QRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRREnctLDTECHEKEKHINQLQTK 288
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE---LARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 289 VAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLM----- 363
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLealra 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 364 --GKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNK 441
Cdd:COG1196 395 aaELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250
....*....|.
gi 575771867 442 ELNENQLVRKQ 452
Cdd:COG1196 475 LEAALAELLEE 485
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
272-520 |
1.36e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 272 DTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELlkaNEI 351
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 352 IKKLQ---------------GDLKTLMGKLKLKNTVTIQQEKLLAE---KEEMLQKERKESQDAGQFLRAKEQEVCRLQE 413
Cdd:COG3883 92 ARALYrsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLEElkaDKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 414 QLETTVQKLEESKQLLKNNEK-LITWLNKELNENQLVRKQDTLGTSATPHSTSNSTIRSGLSPNLNVVDRLNYPSCGIGY 492
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAaAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
250 260
....*....|....*....|....*...
gi 575771867 493 PVSSALTFQNAFPHVVAAKNTSHPISGP 520
Cdd:COG3883 252 AGAAGAAAGSAGAAGAAAGAAGAGAAAA 279
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
214-443 |
1.82e-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: 56.70 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 214 QLQSRLSELEAANKELTERKYKgdstVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLE 293
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKE----LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 294 QEIKDKDQLvlrtkeafdtIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVT 373
Cdd:COG4942 97 AELEAQKEE----------LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 374 IQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKEL 443
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
122-455 |
9.07e-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: 9.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 122 LKCSKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNkhsqeLTAEKEKALQTQVQCQQQHEQQK 201
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ-----LKDEQNKIKKQLSEKQKELEQNN 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 202 KELETLhQRNIHQLQSRLSEL-----EAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECH 276
Cdd:TIGR04523 281 KKIKEL-EKQLNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENS 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 277 EKEKHINQLQTKVAVLEQEIKDKDQ----LVLRTKEAFDTIQEQKVA---LEENGEKNQIQLGKLEATIKSLSAELLKAN 349
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQeiknLESQINDLESKIQNQEKLnqqKDEQIKKLQQEKELLEKEIERLKETIIKNN 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 350 EIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQ---LETTVQKLEESK 426
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEkkeLEEKVKDLTKKI 519
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 575771867 427 QLLKNN-----------EKLITWLNKELNENQLVRKQDTL 455
Cdd:TIGR04523 520 SSLKEKieklesekkekESKISDLEDELNKDDFELKKENL 559
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
215-443 |
1.03e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 215 LQSRLSELEAANKELTERKYkgdstvrELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQ 294
Cdd:TIGR02169 665 GILFSRSEPAELQRLRERLE-------GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 295 EIKDK-------DQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEAT-----IKSLSAELLKANEIIKKLQGDLKTL 362
Cdd:TIGR02169 738 RLEELeedlsslEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 363 MGKLklkntvtiqqeKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETtvqKLEESKQLLKNNEKLITWLNKE 442
Cdd:TIGR02169 818 EQKL-----------NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG---KKEELEEELEELEAALRDLESR 883
|
.
gi 575771867 443 L 443
Cdd:TIGR02169 884 L 884
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
214-427 |
1.03e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.02 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 214 QLQSRLSELEAANKELTERkykgdstVRELKAKLAGVEEELQ--RAKQEVLSLRRENCTLDTEchekekhINQLQTKVAV 291
Cdd:COG3206 165 NLELRREEARKALEFLEEQ-------LPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQ-------LSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 292 LEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQI--QLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK-- 367
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLraQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQqe 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575771867 368 -------LKNTVTI--QQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQ 427
Cdd:COG3206 311 aqrilasLEAELEAlqAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
125-453 |
1.73e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 125 SKEEKLS-LTRSLDDVTRQL------HITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKalqtqvqcqqqh 197
Cdd:PRK03918 335 EKEERLEeLKKKLKELEKRLeeleerHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE------------ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 198 eqQKKELETLHQRnIHQLQSRLSELEAANKELTERKYKGDSTVREL------------KAKLAGVEEELQRAKQEVLSLR 265
Cdd:PRK03918 403 --IEEEISKITAR-IGELKKEIKELKKAIEELKKAKGKCPVCGRELteehrkelleeyTAELKRIEKELKEIEEKERKLR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 266 RENCTLDTECHEKEKHINQLQTkvavLEQEIKDKDQLvlrtkEAFDtIQEQKVALEENgEKNQIQLGKLEATIKSLSAEL 345
Cdd:PRK03918 480 KELRELEKVLKKESELIKLKEL----AEQLKELEEKL-----KKYN-LEELEKKAEEY-EKLKEKLIKLKGEIKSLKKEL 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 346 LKANEIIKKL----------QGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQL 415
Cdd:PRK03918 549 EKLEELKKKLaelekkldelEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEEL 628
|
330 340 350
....*....|....*....|....*....|....*...
gi 575771867 416 ETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQD 453
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE 666
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
225-384 |
3.39e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.24 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 225 ANKELTERKYKGDSTVRELKAKL-AGVEEELQRAKQEVLSLRREnctLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLV 303
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKEAeAIKKEALLEAKEEIHKLRNE---FEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 304 LRTKEAFDtiqeqkvALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGD------LKTLMGKLKLKNTVTIQQE 377
Cdd:PRK12704 106 EKREEELE-------KKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEeakeilLEKVEEEARHEAAVLIKEI 178
|
....*..
gi 575771867 378 KLLAEKE 384
Cdd:PRK12704 179 EEEAKEE 185
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
237-408 |
3.54e-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: 51.46 E-value: 3.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 237 DSTVRELKAKLAGVEEELQRAKQEVLSLRrenctldTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ 316
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALE-------ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 317 K--VALeengeknQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKlkntvtiQQEKLLAEKEEMLQKERKES 394
Cdd:COG1579 89 KeyEAL-------QKEIESLKRRISDLEDEILELMERIEELEEELAELEAELA-------ELEAELEEKKAELDEELAEL 154
|
170
....*....|....
gi 575771867 395 QDAGQFLRAKEQEV 408
Cdd:COG1579 155 EAELEELEAEREEL 168
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
215-435 |
4.03e-07 |
|
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: 52.98 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 215 LQSRLSELEAANKELterkykgdstVRELKAKLAGVEEELQRAKqevlslrRENCTLDTECHEKEKHINQLQTKVAVLEQ 294
Cdd:pfam07888 32 LQNRLEECLQERAEL----------LQAQEAANRQREKEKERYK-------RDREQWERQRRELESRVAELKEELRQSRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 295 EIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTI 374
Cdd:pfam07888 95 KHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 575771867 375 QQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKL 435
Cdd:pfam07888 175 QLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
125-436 |
1.10e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 125 SKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEwashtasLTNKHSQELTAEKEKAlqtqvqcqqQHEQQKKEL 204
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEELKEE-------IEELEKELESLEGSKR---------KLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 205 EtlhqRNIHQLQSRLSELEAANKELTERKYKGDSTVR------ELKAKLAGVEEELQRAKQEVLSLRRENctldTECHEK 278
Cdd:PRK03918 265 E----ERIEELKKEIEELEEKVKELKELKEKAEEYIKlsefyeEYLDELREIEKRLSRLEEEINGIEERI----KELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 279 EKHINQLQTKvavlEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQI-QLGKLEATIKSLSAELLKANEIIKKLQG 357
Cdd:PRK03918 337 EERLEELKKK----LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 575771867 358 DLKTLMGKLKLKNTVTIQQEKllAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLI 436
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKK--AKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL 489
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
118-359 |
2.16e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 118 LAGCLKCSKEEKLSLTRSLDDVTRQLHITQETLSEK---MQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQ 194
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELekrLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 195 QQHEQQKKELETLHQR------NIHQLQSRLSELEAANKELTERK------YKGDSTVRE-LKAKLAGVEEELQRAKQEV 261
Cdd:TIGR02169 308 RSIAEKERELEDAEERlakleaEIDKLLAEIEELEREIEEERKRRdklteeYAELKEELEdLRAELEEVDKEFAETRDEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 262 LSLRREnctLDTECHEKEKHIN----------QLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQL 331
Cdd:TIGR02169 388 KDYREK---LEKLKREINELKReldrlqeelqRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
250 260
....*....|....*....|....*...
gi 575771867 332 GKLEATIKSLSAELLKANEIIKKLQGDL 359
Cdd:TIGR02169 465 SKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
135-445 |
3.92e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 135 SLDDVTRQLHITQETlsEKMQELDKLRSEWASHTASLTNKHSQELTAEKekALQTQVQCQQQHEQQKKELETLHQrNIHQ 214
Cdd:PRK02224 188 SLDQLKAQIEEKEEK--DLHERLNGLESELAELDEEIERYEEQREQARE--TRDEADEVLEEHEERREELETLEA-EIED 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 215 LQSRLSELEAANKELTERKYKGDSTVRELKAKLAGV--EEELQRAKQEVLSLRRE--------------NCTLDTECHEK 278
Cdd:PRK02224 263 LRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADAEAVEARREeledrdeelrdrleECRVAAQAHNE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 279 E-----KHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQ-------IQLGKLEATIKSLSAELL 346
Cdd:PRK02224 343 EaeslrEDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRerfgdapVDLGNAEDFLEELREERD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 347 KANEIIKKLQGDLKTLMGKLKLKNTV--------------------TI-----QQEKLLAEKEEM--LQKERKESQDAGQ 399
Cdd:PRK02224 423 ELREREAELEATLRTARERVEEAEALleagkcpecgqpvegsphveTIeedreRVEELEAELEDLeeEVEEVEERLERAE 502
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 575771867 400 FLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNE 445
Cdd:PRK02224 503 DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
214-457 |
4.18e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 214 QLQSRLSELEAANKELterkykgdstvRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLE 293
Cdd:COG4372 32 QLRKALFELDKLQEEL-----------EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 294 QEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVT 373
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 374 IQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQD 453
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
....
gi 575771867 454 TLGT 457
Cdd:COG4372 261 EELE 264
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
182-350 |
4.39e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 182 EKEKALQTQVQCQQQHEQQKKELETLHQRnIHQLQSRLSELEAANKELT--ERKYKGDSTVRELKAKLAGVEEELQRAKQ 259
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEE-LEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 260 EVLSLRRenctLDTECHEKEKHINQLQTKVAVLEQEIK-DKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATI 338
Cdd:COG4717 154 RLEELRE----LEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170
....*....|..
gi 575771867 339 KSLSAELLKANE 350
Cdd:COG4717 230 EQLENELEAAAL 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
155-417 |
5.20e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 155 QELDKLRSEWASHTASLtnkhsQELTAEKEKALQTQVQCQQQHEQQKKELETL-HQRNIHQLQSRLSELEAANKELterk 233
Cdd:COG4913 617 AELAELEEELAEAEERL-----EALEAELDALQERREALQRLAEYSWDEIDVAsAEREIAELEAELERLDASSDDL---- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 234 ykgdstvRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIkdKDQLVLRTKEAFDTI 313
Cdd:COG4913 688 -------AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA--RLELRALLEERFAAA 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 314 QEQKV------ALEENGEKNQIQLGKLEATI---------------KSLSAELLKANEIIKKLQgdlktlmgklklkntv 372
Cdd:COG4913 759 LGDAVerelreNLEERIDALRARLNRAEEELeramrafnrewpaetADLDADLESLPEYLALLD---------------- 822
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 575771867 373 TIQQEKLLAEKEEMLQ-KERKESQDAGQFLRAKEQEVCRLQEQLET 417
Cdd:COG4913 823 RLEEDGLPEYEERFKElLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| HD_XRCC4-like_N |
cd22210 |
N-terminal head domain found in the XRCC4 superfamily of proteins; The XRCC4 superfamily ... |
9-109 |
9.37e-06 |
|
N-terminal head domain found in the XRCC4 superfamily of proteins; The XRCC4 superfamily includes five families: XRCC4, XLF, PAXX, SAS6 and CCDC61. XRCC4 (X-ray repair cross-complementing protein 4), XLF (XRCC4-like factor) and PAXX (paralog of XRCC4 and XLF) play crucial roles in the non-homologous end-joining (NHEJ) DNA repair pathway. SAS6 (spindle assembly abnormal protein 6) and CCDC61 (coiled-coil domain-containing protein 61) have a centrosomal/centriolar function. Members of this superfamily have an N-terminal globular head domain, a centrally located coiled-coil, and a C-terminal low-complexity region. They form homodimers through two homodimerization domains: an N-terminal globular head domain and a parallel coiled-coil domain. In addition, some members such as XRCC4 and XLF form symmetric heterodimers that interact through their globular head domains at the opposite end of the homodimer interface, and may form XLF-XRCC4 filaments. This model corresponds to the N-terminal head domain of XRCC4 superfamily proteins.
Pssm-ID: 408999 Cd Length: 115 Bit Score: 45.22 E-value: 9.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 9 LVIRLTDDtdpFFLYNLVISEEDFQSLKLQQGLLVDFLAFPQKFIDLLQQCmqehAKETPRFLLQLlssaTLLENSPVLl 88
Cdd:cd22210 28 LRLHVSDD---AFLWTGEVSESDISQLKNDQGILVDFASFPGKLRSALEKC----ILASDRFTFVL----TIRGDEAYL- 95
|
90 100
....*....|....*....|.
gi 575771867 89 nVVETNPFKHLIHLSLKLLPG 109
Cdd:cd22210 96 -KLVEILDEQLPHITFALRKV 115
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
282-452 |
1.12e-05 |
|
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: 47.84 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 282 INQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKT 361
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 362 LMGKLKlKNTVTIQQ------EKLLAEKEEMLQKER---------KESQDAGQFLRAKEQEVCRLQEQLETTVQKLEesk 426
Cdd:COG4942 102 QKEELA-ELLRALYRlgrqppLALLLSPEDFLDAVRrlqylkylaPARREQAEELRADLAELAALRAELEAERAELE--- 177
|
170 180
....*....|....*....|....*.
gi 575771867 427 QLLKNNEKLITWLNKELNENQLVRKQ 452
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLAR 203
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
202-441 |
1.13e-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: 48.63 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 202 KELETLHQRNIHQLQSRLSELEAANKELTERKYKGD---STVRELKAKLAGVEEELQRAKQEvlslrrenctLDTECHEK 278
Cdd:pfam01576 18 KERQQKAESELKELEKKHQQLCEEKNALQEQLQAETelcAEAEEMRARLAARKQELEEILHE----------LESRLEEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 279 EKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGD 358
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 359 LKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESK-QLLKNNEKLIT 437
Cdd:pfam01576 168 LAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRaQLAKKEEELQA 247
|
....
gi 575771867 438 WLNK 441
Cdd:pfam01576 248 ALAR 251
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
201-426 |
1.14e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 201 KKELETLHQRNiHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQR----------AKQEVLSLRRENCT 270
Cdd:PRK03918 178 IERLEKFIKRT-ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEleelkeeieeLEKELESLEGSKRK 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 271 LDTECHEKEKHINQLQTKVAVLEQ------EIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAE 344
Cdd:PRK03918 257 LEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 345 LLKANEIIKKLQG----------------DLKTLMGKL-KLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQE 407
Cdd:PRK03918 337 EERLEELKKKLKElekrleeleerhelyeEAKAKKEELeRLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
250
....*....|....*....
gi 575771867 408 VCRLQEQLETTVQKLEESK 426
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAK 435
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
201-450 |
1.87e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 47.61 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 201 KKELETLHQRNIHQLQSRLSEL-----EAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLslrrenctldtec 275
Cdd:PRK05771 37 KEELSNERLRKLRSLLTKLSEAldklrSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIK------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 276 hEKEKHINQLQTKVAVLEQEIKDKDQLvlrtkEAFDTiqeqKVALEENGEKNQIQLGKLEATIKS-LSAELLKANEIIKK 354
Cdd:PRK05771 104 -ELEEEISELENEIKELEQEIERLEPW-----GNFDL----DLSLLLGFKYVSVFVGTVPEDKLEeLKLESDVENVEYIS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 355 lqgdlktlmgKLKLKNTVTIQQEKLLAEK-EEMLQK---ERKESQDAG---QFLRAKEQEVCRLQEQLETTVQKLEESKQ 427
Cdd:PRK05771 174 ----------TDKGYVYVVVVVLKELSDEvEEELKKlgfERLELEEEGtpsELIREIKEELEEIEKERESLLEELKELAK 243
|
250 260
....*....|....*....|...
gi 575771867 428 llKNNEKLITWlnKELNENQLVR 450
Cdd:PRK05771 244 --KYLEELLAL--YEYLEIELER 262
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
131-366 |
1.96e-05 |
|
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: 47.07 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 131 SLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLtnkhsqeltAEKEKALQTQVQCQQQHEQQKKELETLHQR 210
Cdd:COG4942 59 ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL---------EAQKEELAELLRALYRLGRQPPLALLLSPE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 211 NIHQLQSRLSELEAANKELTERkykgdstVRELKAKLagveEELQRAKQEvlslrrenctLDTECHEKEKHINQLQTKVA 290
Cdd:COG4942 130 DFLDAVRRLQYLKYLAPARREQ-------AEELRADL----AELAALRAE----------LEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575771867 291 VLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKnqiqlgkLEATIKSLSAELLKANEiiKKLQGDLKTLMGKL 366
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEE-------LEALIARLEAEAAAAAE--RTPAAGFAALKGKL 255
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
176-447 |
2.77e-05 |
|
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: 47.27 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 176 SQELTAEKEKALQTQVQCQQQHEQQKKELETLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKaklagVEEELQ 255
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK-----LNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 256 RAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLE-QEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKL 334
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEeKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 335 EATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQ----QEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCR 410
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEleklQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
250 260 270
....*....|....*....|....*....|....*..
gi 575771867 411 LQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQ 447
Cdd:pfam02463 400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEE 436
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
151-449 |
3.37e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 151 SEKMQELDKlRSEWASHTASLTNKHSQELTAE--KEKA--LQTQVQCQQQHEQQKKELETLHQRNIHQLQSRLSELEAAN 226
Cdd:PTZ00121 1456 AKKAEEAKK-KAEEAKKADEAKKKAEEAKKADeaKKKAeeAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 227 KELTERKYKGDSTVREL-KAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLR 305
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK 1614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 306 TKEAfdTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEE 385
Cdd:PTZ00121 1615 AEEA--KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575771867 386 MLQKERKESQDAGQfLRAKEQEVCRLQEQL----ETTVQKLEESKQLLKNNEKLITWLNKELNENQLV 449
Cdd:PTZ00121 1693 ALKKEAEEAKKAEE-LKKKEAEEKKKAEELkkaeEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
180-452 |
4.06e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 180 TAEKEKALQTQVQCQQQHEQQKKELETLHQRnIHQLQSRLSELEAANKELTERKYKGDSTVRE----LKAKLAGVEEELQ 255
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLKEL-AEQLKELEEKLKKYNLEELEKKAEEYEKLKEklikLKGEIKSLKKELE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 256 RAKQevlsLRRENCTLDTECHEKEKHINQLQTKVAVLEQE-IKDKDQLVLRTKEAFDTIQEQKVALEEngeknqiqLGKL 334
Cdd:PRK03918 550 KLEE----LKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPFYNEYLELKDAEKE--------LERE 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 335 EATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNtVTIQQEKLLAEKEEMLQKERKESQdagqfLRAKEQEVCRLQEQ 414
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELE-KKYSEEEYEELREEYLELSRELAG-----LRAELEELEKRREE 691
|
250 260 270
....*....|....*....|....*....|....*...
gi 575771867 415 LETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 452
Cdd:PRK03918 692 IKKTLEKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
148-447 |
6.34e-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: 46.26 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 148 ETL-SEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQK------KELETLHQRNIHQLQSRLS 220
Cdd:pfam15921 248 EALkSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEiiqeqaRNQNSMYMRQLSDLESTVS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 221 ELEAankELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDtechekekhiNQLQTKVAVLEQeikdkd 300
Cdd:pfam15921 328 QLRS---ELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD----------DQLQKLLADLHK------ 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 301 qlvlRTKEaFDTIQEQKVALEENGEKNQIqlgkleaTIKSLSAELLKANEIIKKLQGDLKTlmgklkLKNTVTIQQEKLL 380
Cdd:pfam15921 389 ----REKE-LSLEKEQNKRLWDRDTGNSI-------TIDHLRRELDDRNMEVQRLEALLKA------MKSECQGQMERQM 450
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575771867 381 AEKEEMLQKERKESQDAGQFLRAKeqevcrlqEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQ 447
Cdd:pfam15921 451 AAIQGKNESLEKVSSLTAQLESTK--------EMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE 509
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
127-434 |
9.32e-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: 45.55 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 127 EEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLR----SEWASHTASLTN---KHSQELTAEKEKaLQTQVQCQQQHEQ 199
Cdd:pfam01576 299 EELEALKTELEDTLDTTAAQQELRSKREQEVTELKkaleEETRSHEAQLQEmrqKHTQALEELTEQ-LEQAKRNKANLEK 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 200 QKKELETLHQrnihQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKE 279
Cdd:pfam01576 378 AKQALESENA----ELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 280 KHINQLQTKVAVLEQEIKDKDQLV---LRTKEAFDT----IQEQKVALEENGEKNQIQLGKLEATIKSLSAELLkanEII 352
Cdd:pfam01576 454 GKNIKLSKDVSSLESQLQDTQELLqeeTRQKLNLSTrlrqLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLS---DMK 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 353 KKLQGDLKTLMGKLKLKntvtiqqEKLLAEKEEMLQKERKESQDAGQFLRAKEqevcRLQEQLETTVQKLEESKQLLKNN 432
Cdd:pfam01576 531 KKLEEDAGTLEALEEGK-------KRLQRELEALTQQLEEKAAAYDKLEKTKN----RLQQELDDLLVDLDHQRQLVSNL 599
|
..
gi 575771867 433 EK 434
Cdd:pfam01576 600 EK 601
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
169-427 |
9.81e-05 |
|
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: 45.14 E-value: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 169 ASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELetlhQRNIHQLQSRLSELEAANKELTERkykgdstVRELKAKLA 248
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARR-------IRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 249 GVEEELQRAKQEVLSLRREnctLDTECHEKEKHINQLQTkvavleQEIKDKDQLVLRTKEAFDTIQEQKV------ALEE 322
Cdd:COG4942 80 ALEAELAELEKEIAELRAE---LEAQKEELAELLRALYR------LGRQPPLALLLSPEDFLDAVRRLQYlkylapARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 323 NGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgklklkntvtiqqEKLLAEKEEMLQKERKESQDAGQFLR 402
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAAL--------------EALKAERQKLLARLEKELAELAAELA 216
|
250 260
....*....|....*....|....*
gi 575771867 403 AKEQEVCRLQEQLETTVQKLEESKQ 427
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
147-398 |
1.01e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 147 QETLSEKMQELDKLRSEwashtASLTNKHSQELTAEKEKALqtqvqcqqqheqqkKELETLhQRNIHQLQSRLSELEAAN 226
Cdd:COG4942 19 ADAAAEAEAELEQLQQE-----IAELEKELAALKKEEKALL--------------KQLAAL-ERRIAALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 227 KELTERkykgdstVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKE----KHINQLQTKVAVLEQEIKDKDQL 302
Cdd:COG4942 79 AALEAE-------LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 303 VLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAE 382
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250
....*....|....*.
gi 575771867 383 KEEMLQKERKESQDAG 398
Cdd:COG4942 232 LEAEAAAAAERTPAAG 247
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
201-391 |
1.04e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 201 KKELETLHQRNIHQLQSRLSELEAANKELTERKykgdSTVRELKAKLAGVEEELQRAKQEVLSLRRE---------NCTL 271
Cdd:COG4717 55 ADELFKPQGRKPELNLKELKELEEELKEAEEKE----EEYAELQEELEELEEELEELEAELEELREEleklekllqLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 272 DTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQI----QLGKLEATIKSLSAELLK 347
Cdd:COG4717 131 YQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLateeELQDLAEELEELQQRLAE 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 575771867 348 ANEIIKKLQGDLKTLMGKLKlkntvTIQQEKLLAEKEEMLQKER 391
Cdd:COG4717 211 LEEELEEAQEELEELEEELE-----QLENELEAAALEERLKEAR 249
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
126-321 |
1.24e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 126 KEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKAlqtqvQCQQQHEQQKKELE 205
Cdd:COG1196 336 EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA-----ELAAQLEELEEAEE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 206 TLHQRnIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQL 285
Cdd:COG1196 411 ALLER-LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
170 180 190
....*....|....*....|....*....|....*.
gi 575771867 286 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALE 321
Cdd:COG1196 490 AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
122-423 |
1.58e-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: 45.11 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 122 LKCSKEEKLSLTRSLDDVTRQLHITQETLSE-------KMQELDKLRSEwashtasltNKHSQELTAEKEKALQTQVQCQ 194
Cdd:pfam15921 491 LESSERTVSDLTASLQEKERAIEATNAEITKlrsrvdlKLQELQHLKNE---------GDHLRNVQTECEALKLQMAEKD 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 195 QQHEQQKKELETL------HQRNIHQLQSRLSELEaanKELTER----------KYKGDSTVRELKAKLAGVEEE---LQ 255
Cdd:pfam15921 562 KVIEILRQQIENMtqlvgqHGRTAGAMQVEKAQLE---KEINDRrlelqefkilKDKKDAKIRELEARVSDLELEkvkLV 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 256 RAKQE----VLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDK--------DQLVLRTKEAFDTIQEQKVALEEN 323
Cdd:pfam15921 639 NAGSErlraVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKseemetttNKLKMQLKSAQSELEQTRNTLKSM 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 324 ------------GEKNQI-----QLGKLEATIKSLSAELLKAN-------EIIKKLQGDLKTLM---GKLKLKNTVTIQQ 376
Cdd:pfam15921 719 egsdghamkvamGMQKQItakrgQIDALQSKIQFLEEAMTNANkekhflkEEKNKLSQELSTVAtekNKMAGELEVLRSQ 798
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 575771867 377 EKLLAEK----EEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLE 423
Cdd:pfam15921 799 ERRLKEKvanmEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
203-298 |
1.68e-04 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 43.03 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 203 ELETlHQRNIHQLQSRLSEL----EAANKELTERKyKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEK 278
Cdd:pfam05266 79 ELEK-HGFDVKAPQSRINKLlslkDRQTKLLEELK-KLEKKIAEEESEKRKLEEEIDELEKKILELERQLALAKEKKEAA 156
|
90 100
....*....|....*....|
gi 575771867 279 EKHINQLQTKVAVLEQEIKD 298
Cdd:pfam05266 157 DKEIARLKSEAEKLEQEIQD 176
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
113-443 |
1.75e-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: 44.63 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 113 EIKKFLAGCLKCSKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKA------ 186
Cdd:TIGR04523 307 DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQsykqei 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 187 --LQTQVQCQQQHEQQKKELETLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQrakqevlSL 264
Cdd:TIGR04523 387 knLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK-------NL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 265 RRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAE 344
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 345 LLKANEIIKKLQGDLK-TLMGKLKLKNTVTIQQ-----EKLLA---EKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQL 415
Cdd:TIGR04523 540 ISDLEDELNKDDFELKkENLEKEIDEKNKEIEElkqtqKSLKKkqeEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL 619
|
330 340
....*....|....*....|....*...
gi 575771867 416 ETTVQKLEESKQLLKNNEKLITWLNKEL 443
Cdd:TIGR04523 620 EKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
131-331 |
1.94e-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: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 131 SLTRSLDDVTRQLHITQETLSEKMQELDKLRSE----WASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELET 206
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 207 LHQ--------RNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVL-SLRRENCTLDTECHE 277
Cdd:COG3206 252 GPDalpellqsPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILaSLEAELEALQAREAS 331
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 575771867 278 KEKHINQLQTKVAVL---EQEIKDKDQLVLRTKEAFDTIQE--QKVALEENGEKNQIQL 331
Cdd:COG3206 332 LQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQrlEEARLAEALTVGNVRV 390
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
216-424 |
3.99e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 216 QSRLSELEAANKELTERkykgdstVRELKAKLAGVEEELQRAKQevlslRRENCTLDTECHEKEKHINQLQTKVAVLEQE 295
Cdd:COG4913 609 RAKLAALEAELAELEEE-------LAEAEERLEALEAELDALQE-----RREALQRLAEYSWDEIDVASAEREIAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 296 IKDkdqlVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgklklkntVTIQ 375
Cdd:COG4913 677 LER----LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA---------EDLA 743
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 575771867 376 QEKLLAEKEEMLQKERKEsQDAGQFLRAKEQEVCRLQEQLETTVQKLEE 424
Cdd:COG4913 744 RLELRALLEERFAAALGD-AVERELRENLEERIDALRARLNRAEEELER 791
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
133-331 |
4.53e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 133 TRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLtNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETLhQRNI 212
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI-EKEIENLNGKKEELEEELEELEAALRDLESRLGDL-KKER 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 213 HQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELqrakQEVLSLRREnctlDTECHEKEKHINQLQTKVAVL 292
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL----SEIEDPKGE----DEEIPEEELSLEDVQAELQRV 963
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 575771867 293 EQEIKDKDQLVLR-------TKEAFDTIQEQKVALEEngEKNQIQL 331
Cdd:TIGR02169 964 EEEIRALEPVNMLaiqeyeeVLKRLDELKEKRAKLEE--ERKAILE 1007
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
208-447 |
6.34e-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: 42.80 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 208 HQRNI--HQLQSRLSELEAAN-KELTERKYKGDSTVRELKAKLAGVEEELQR-----AKQEVLSLRRENCTLDTECHEKE 279
Cdd:pfam17380 280 HQKAVseRQQQEKFEKMEQERlRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaiyAEQERMAMERERELERIRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 280 KHINQL-QTKVAVLEQEIKDKDQLVL-------RTKEAFDTIQEQKVALEENGEKNQIQLGKLEatikSLSAELLKANEI 351
Cdd:pfam17380 360 RELERIrQEEIAMEISRMRELERLQMerqqkneRVRQELEAARKVKILEEERQRKIQQQKVEME----QIRAEQEEARQR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 352 -IKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQdagqflraKEQEVCRLQEQLETTV--QKLEESKQL 428
Cdd:pfam17380 436 eVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE--------KEKRDRKRAEEQRRKIleKELEERKQA 507
|
250
....*....|....*....
gi 575771867 429 LKNNEKLITWLNKELNENQ 447
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQ 526
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
313-445 |
6.83e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 313 IQEQKVALEENGEKNQIQLGKLEAtiKSLSAE-LLKANEIIKKLQGDLKTlmgKLKLKNTVTIQQEKLLAEKEEMLqKER 391
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEA--EAIKKEaLLEAKEEIHKLRNEFEK---ELRERRNELQKLEKRLLQKEENL-DRK 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 575771867 392 KESqdagqfLRAKEQEvcrLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNE 445
Cdd:PRK12704 102 LEL------LEKREEE---LEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
237-457 |
9.00e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 237 DSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ 316
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 317 KVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK-LKNTVTIQQEKLLAEKEEMLQKERKESQ 395
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLEsLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 575771867 396 DAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQDTLGT 457
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
219-442 |
9.30e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 219 LSELEAANKELteRKYKGDSTVRELKaKLAGVEEELQRAKQEVLSLRRenctLDTECHEKEKHINQLQTKVAVLEQEIKD 298
Cdd:COG4717 48 LERLEKEADEL--FKPQGRKPELNLK-ELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 299 KDQLvlrtKEAFDTIQEQKvALEENGEKNQIQLGKLEA---TIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQ 375
Cdd:COG4717 121 LEKL----LQLLPLYQELE-ALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 575771867 376 QeklLAEKEEMLQKERKEsqdagqflrakeqevcrLQEQLETTVQKLEESKQLLKNNEKLITWLNKE 442
Cdd:COG4717 196 D---LAEELEELQQRLAE-----------------LEEELEEAQEELEELEEELEQLENELEAAALE 242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
148-453 |
1.02e-03 |
|
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: 42.34 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 148 ETLSEKMQELDKLRSEWASHTASLTNKHS-QELTAEKEKALQTQVQCQQQHEQQKKELETlHQRNIHQLQSRLSELEAAN 226
Cdd:TIGR00606 795 ERFQMELKDVERKIAQQAAKLQGSDLDRTvQQVNQEKQEKQHELDTVVSKIELNRKLIQD-QQEQIQHLKSKTNELKSEK 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 227 KELTERKYKGDSTVRELKAKLAGVEE---ELQRAKQEVLSLRRencTLDTECHEKEKHINQLQTKVAVLEQEIKDK---- 299
Cdd:TIGR00606 874 LQIGTNLQRRQQFEEQLVELSTEVQSlirEIKDAKEQDSPLET---FLEKDQQEKEELISSKETSNKKAQDKVNDIkekv 950
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 300 DQLVLRTKEAFDTIQEQKvaleengeknQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNtvtiQQEKL 379
Cdd:TIGR00606 951 KNIHGYMKDIENKIQDGK----------DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK----IQERW 1016
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575771867 380 LaEKEEMLQKERKESQDAGQFLRAKEQEVCRLQ-EQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLVRKQD 453
Cdd:TIGR00606 1017 L-QDNLTLRKRENELKEVEEELKQHLKEMGQMQvLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKE 1090
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
125-416 |
1.04e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 125 SKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASL--TNKHSQELTAEKEKALQTQVQCQQQHEQQKK 202
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELeqLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 203 ELETLHQRnIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKE--K 280
Cdd:COG4372 109 EAEELQEE-LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAldE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 281 HINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLK 360
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 575771867 361 TLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLE 416
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
113-447 |
1.45e-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: 41.88 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 113 EIKKFLAGCLKCSKEEKLSLTRSLDDVTRQLHITQETLSEKMQEL-DKLRSEWASHTASLTNKHSQELTAEKEKALQTQV 191
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLrEALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 192 QCQQQHEQQKKELETLHQR-NIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCT 270
Cdd:TIGR00618 267 ARIEELRAQEAVLEETQERiNRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 271 LDTeCHEKEKHINQlQTKVAVLEQEIKDKdQLVLRtkEAFDTIQEQKVALEENgeknqiqlgkleatIKSLSAELlkanE 350
Cdd:TIGR00618 347 LQT-LHSQEIHIRD-AHEVATSIREISCQ-QHTLT--QHIHTLQQQKTTLTQK--------------LQSLCKEL----D 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 351 IIKKLQGDLKTLMGKLKlkntvTIQQEKLLAEKEEMLQKERKE-----SQDAGQFLRAKEQEVCRLQEQLETTVQKLEES 425
Cdd:TIGR00618 404 ILQREQATIDTRTSAFR-----DLQGQLAHAKKQQELQQRYAElcaaaITCTAQCEKLEKIHLQESAQSLKEREQQLQTK 478
|
330 340
....*....|....*....|..
gi 575771867 426 KQLLKNNEKLITWLNKELNENQ 447
Cdd:TIGR00618 479 EQIHLQETRKKAVVLARLLELQ 500
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
184-326 |
2.25e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 184 EKALQTQVQCQQQHEQQKKELETLH-QRNIHQLQSRLSELEAANKELteRKYkgdstVRELKAKLAGVEEELQRAKQEVL 262
Cdd:COG2433 379 EEALEELIEKELPEEEPEAEREKEHeERELTEEEEEIRRLEEQVERL--EAE-----VEELEAELEEKDERIERLERELS 451
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 575771867 263 SLRREnctLDTEcHEKEKHINQLQTKVAVLEQEIKDKDQlvlRTKEAFDTIQEQK--VALEENGEK 326
Cdd:COG2433 452 EARSE---ERRE-IRKDREISRLDREIERLERELEEERE---RIEELKRKLERLKelWKLEHSGEL 510
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
127-437 |
2.61e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.88 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 127 EEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELE- 205
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELEl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 206 --------------TLHQRNIHQLQSRLSELEAANKELTERKYKgdstVRELKAKLAGVE---EELQRAKQEVLSLRREN 268
Cdd:pfam05557 128 qstnseleelqerlDLLKAKASEAEQLRQNLEKQQSSLAEAEQR----IKELEFEIQSQEqdsEIVKNSKSELARIPELE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 269 CTLDtECHEKEKHINQLQTKVAVLEQEIKDkdqlvLRTK-EAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLK 347
Cdd:pfam05557 204 KELE-RLREHNKHLNENIENKLLLKEEVED-----LKRKlEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 348 ----ANEIIKKLQGDLkTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLE 423
Cdd:pfam05557 278 pedlSRRIEQLQQREI-VLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERD 356
|
330
....*....|....
gi 575771867 424 ESKQLLKNNEKLIT 437
Cdd:pfam05557 357 GYRAILESYDKELT 370
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
231-445 |
2.90e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 231 ERKYKGDSTV-RELKAKLAGVEEELQRaKQEVLSLRRENctlDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLR---T 306
Cdd:PRK03918 161 ENAYKNLGEViKEIKRRIERLEKFIKR-TENIEELIKEK---EKELEEVLREINEISSELPELREELEKLEKEVKEleeL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 307 KEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKklqgDLKTLMGKLKlkntvtiQQEKLLAEKEEM 386
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK----ELKELKEKAE-------EYIKLSEFYEEY 305
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 575771867 387 LQKERKESQDAGQFlrakEQEVCRLQEQLEttvqKLEESKQLLKNNEKLITWLNKELNE 445
Cdd:PRK03918 306 LDELREIEKRLSRL----EEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEE 356
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
202-367 |
2.94e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 202 KELETLHQRnIHQLQSRLSELEAANKELteRKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKH 281
Cdd:COG4913 255 EPIRELAER-YAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 282 INQ--------LQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQ----LGKLEATIKSLSAELLKAN 349
Cdd:COG4913 332 IRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEaaalLEALEEELEALEEALAEAE 411
|
170
....*....|....*...
gi 575771867 350 EIIKKLQGDLKTLMGKLK 367
Cdd:COG4913 412 AALRDLRRELRELEAEIA 429
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
141-387 |
3.05e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.59 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 141 RQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKELETL--HQRNIHQLQSR 218
Cdd:pfam12128 276 SRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAaaDQEQLPSWQSE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 219 LSELEAANKELT------ERKYKG--DSTVRELKAKLAGVEEELQRAKQE-VLSLRRENCTLDTECHEKEKHINQLQTKV 289
Cdd:pfam12128 356 LENLEERLKALTgkhqdvTAKYNRrrSKIKEQNNRDIAGIKDKLAKIREArDRQLAVAEDDLQALESELREQLEAGKLEF 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 290 AVLEQEIKDK-DQLVLRTKEAfdTIQEQkvaLEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKL 368
Cdd:pfam12128 436 NEEEYRLKSRlGELKLRLNQA--TATPE---LLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQ 510
|
250
....*....|....*....
gi 575771867 369 KNTVTIQQEKLLAEKEEML 387
Cdd:pfam12128 511 ASRRLEERQSALDELELQL 529
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
201-452 |
3.05e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 201 KKELETLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLR----------RENCT 270
Cdd:TIGR04523 136 NKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllsnlkkkiQKNKS 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 271 LDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAEL----- 345
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLnqlks 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 346 -------LKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETT 418
Cdd:TIGR04523 296 eisdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKL 375
|
250 260 270
....*....|....*....|....*....|....
gi 575771867 419 VQKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 452
Cdd:TIGR04523 376 KKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ 409
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
147-429 |
3.18e-03 |
|
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: 40.58 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 147 QETLSEKMQELDKLRSEWASHTASLTNKHS-----QELTAEKEKALqtqvqcqqqheqqkkelETLHQRNIHQLQSRLSE 221
Cdd:pfam10174 407 QEQLRDKDKQLAGLKERVKSLQTDSSNTDTalttlEEALSEKERII-----------------ERLKEQREREDRERLEE 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 222 LEAANKELterkykgdstvRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLqtkvavlEQEIKDKDQ 301
Cdd:pfam10174 470 LESLKKEN-----------KDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSL-------EIAVEQKKE 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 302 LVLRTKEAFDTIQEQKVALEENGEKNQiqlgkleaTIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLA 381
Cdd:pfam10174 532 ECSKLENQLKKAHNAEEAVRTNPEIND--------RIRLLEQEVARYKEESGKAQAEVERLLGILREVENEKNDKDKKIA 603
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 575771867 382 EKEEMLQKERKESQDAGQFLRAKEQEV--------------------CRLQEQLETTVQKLEESKQLL 429
Cdd:pfam10174 604 ELESLTLRQMKEQNKKVANIKHGQQEMkkkgaqlleearrrednladNSQQLQLEELMGALEKTRQEL 671
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
282-454 |
3.54e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 282 INQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKN---------QIQLGKLEATIKSL---SAELLKAN 349
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvasaEREIAELEAELERLdasSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 350 EIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEvcRLQEQLETTVQKlEESKQLL 429
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA--LLEERFAAALGD-AVERELR 768
|
170 180
....*....|....*....|....*..
gi 575771867 430 KNNEKLITWLNKELN--ENQLVRKQDT 454
Cdd:COG4913 769 ENLEERIDALRARLNraEEELERAMRA 795
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
248-434 |
3.74e-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: 40.34 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 248 AGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKN 327
Cdd:pfam02463 162 AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 328 QIQLGKLE-ATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQ 406
Cdd:pfam02463 242 LQELLRDEqEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321
|
170 180
....*....|....*....|....*...
gi 575771867 407 EVCRLQEQLETTVQKLEESKQLLKNNEK 434
Cdd:pfam02463 322 EKKKAEKELKKEKEEIEELEKELKELEI 349
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
211-455 |
4.02e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.39 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 211 NIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKHINQLQTkva 290
Cdd:TIGR04523 69 KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLT--- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 291 vleqEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKAN---EIIKKLQGDLKTLMGKL- 366
Cdd:TIGR04523 146 ----EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllSNLKKKIQKNKSLESQIs 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 367 KLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVcRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNEN 446
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN-KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDL 300
|
....*....
gi 575771867 447 QLVRKQDTL 455
Cdd:TIGR04523 301 NNQKEQDWN 309
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
134-441 |
4.22e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 134 RSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLT--NKHSQELTAEKEKALQTQVQCQQQHEQQKKELETLHQrN 211
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEavEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE-D 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 212 IHQLQSRL-----------SELEAANKELTERKYKG---DSTVRELKAKLAGVEEELQRAkQEVLSLRRENctlDTECHE 277
Cdd:PRK02224 351 ADDLEERAeelreeaaeleSELEEAREAVEDRREEIeelEEEIEELRERFGDAPVDLGNA-EDFLEELREE---RDELRE 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 278 KEKhinQLQTKVAVLEQEIKDKDQLV-----------LRTKEAFDTIQEQKVALEENGEknqiQLGKLEATIKSLSAELL 346
Cdd:PRK02224 427 REA---ELEATLRTARERVEEAEALLeagkcpecgqpVEGSPHVETIEEDRERVEELEA----ELEDLEEEVEEVEERLE 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 347 KANEIiKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESK 426
Cdd:PRK02224 500 RAEDL-VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN 578
|
330
....*....|....*
gi 575771867 427 QLLKNNEKLITWLNK 441
Cdd:PRK02224 579 SKLAELKERIESLER 593
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
136-446 |
4.73e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 136 LDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEkalqtQVQCQQQHEQQKKELETLHQrNIHQL 215
Cdd:TIGR04523 316 LKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE-----LEEKQNEIEKLKKENQSYKQ-EIKNL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 216 QSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRREnctldtechekekhINQLQTKVAVLEQE 295
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE--------------IKDLTNQDSVKELI 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 296 IKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQ 375
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575771867 376 QEKLLAEKEEMLQK--ERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNEN 446
Cdd:TIGR04523 536 KESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEK 608
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
155-296 |
5.55e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 155 QELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQK-----------KELETLhQRNIHQLQSRLSELE 223
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqlgnvrnnKEYEAL-QKEIESLKRRISDLE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575771867 224 AANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEvlslrrenctLDTECHEKEKHINQLQTKVAVLEQEI 296
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAE----------LDEELAELEAELEELEAEREELAAKI 172
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
214-435 |
6.17e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 214 QLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDT---ECHEKEKHINQL----Q 286
Cdd:COG1340 47 ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKaggSIDKLRKEIERLewrqQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 287 TKVAVLEQEIkdkdQLVLRTKEAFDTIQEQKVALEENGEKNQI---------QLGKLEATIKSLSAELLKANEIIKKLQG 357
Cdd:COG1340 127 TEVLSPEEEK----ELVEKIKELEKELEKAKKALEKNEKLKELraelkelrkEAEEIHKKIKELAEEAQELHEEMIELYK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 358 DLKTLMGKL-KLKNTVTIQQEKLLAEKEEM--LQKERKESQDAGQFLRAKEQEVcRLQEQLETTVQKLEESKQLLKNNEK 434
Cdd:COG1340 203 EADELRKEAdELHKEIVEAQEKADELHEEIieLQKELRELRKELKKLRKKQRAL-KREKEKEELEEKAEEIFEKLKKGEK 281
|
.
gi 575771867 435 L 435
Cdd:COG1340 282 L 282
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
148-440 |
6.25e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 148 ETLSEKMQELDKLRSEWAS---HTASLTNKHsqeltaEKEKALQTQVQCQQQHEQQKKELETLhqrnIHQLQSRLSELEA 224
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDleeEVEEVEERL------ERAEDLVEAEDRIERLEERREDLEEL----IAERRETIEEKRE 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 225 ANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTEchekekhINQLQTKVAVLEqEIKDKDQLVL 304
Cdd:PRK02224 538 RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKER-------IESLERIRTLLA-AIADAEDEIE 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 305 RTKEAFDTIQEQ----KVALEENGEKNQIQLGKL-EATIKSLSAELLKANEIIKKLQGDLKTLMGKL-KLKNTVTIQQEK 378
Cdd:PRK02224 610 RLREKREALAELnderRERLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEEKLDELREERdDLQAEIGAVENE 689
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 575771867 379 LlaEKEEMLQKERKESQDAGQFLRAKEQEVcrlqEQLETTVQKLE-ESKQllKNNEKLITWLN 440
Cdd:PRK02224 690 L--EELEELRERREALENRVEALEALYDEA----EELESMYGDLRaELRQ--RNVETLERMLN 744
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
122-444 |
7.21e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 39.32 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 122 LKCSKEEKLSLTRSLDDVTRQLH---ITQETLSEKMQeldklrsewashtasLTNKHSQELTAEKEKALQTQVQCQQQHE 198
Cdd:pfam05483 284 LKELIEKKDHLTKELEDIKMSLQrsmSTQKALEEDLQ---------------IATKTICQLTEEKEAQMEELNKAKAAHS 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 199 QQKKELETLH--------------QRNIHQLQSRLSELEAANKELTE-RKYKGDSTVR--ELKAKLAGVEEELQRAKQ-- 259
Cdd:pfam05483 349 FVVTEFEATTcsleellrteqqrlEKNEDQLKIITMELQKKSSELEEmTKFKNNKEVEleELKKILAEDEKLLDEKKQfe 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 260 ---EVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKeaFDTIQEQKVALEENGEKNQIQLGKLEA 336
Cdd:pfam05483 429 kiaEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE--LEKEKLKNIELTAHCDKLLLENKELTQ 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 337 TIKSLSAELLKANEII-------KKLQGDLKTLMGK-LKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQF-------- 400
Cdd:pfam05483 507 EASDMTLELKKHQEDIinckkqeERMLKQIENLEEKeMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIeyevlkke 586
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 575771867 401 --LRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELN 444
Cdd:pfam05483 587 kqMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLN 632
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
154-364 |
7.25e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 39.45 E-value: 7.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 154 MQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQheqqKKELETLHQRNIHQLQSRLSELEAANKELTERK 233
Cdd:PLN03229 534 KYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEI----KEKMEALKAEVASSGASSGDELDDDLKEKVEKM 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 234 YKgdstvrELKAKLAGVeeeLQRAKQEVLSLRRENCTLDTECHEKEkhinqLQTKVAVLEQEIKDKDQLVLRTKEAFDTI 313
Cdd:PLN03229 610 KK------EIELELAGV---LKSMGLEVIGVTKKNKDTAEQTPPPN-----LQEKIESLNEEINKKIERVIRSSDLKSKI 675
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 314 QEQKVALEENG------EKNQIQlgKLEATIKSLSAELLKANEIIKK---LQGDLKTLMG 364
Cdd:PLN03229 676 ELLKLEVAKASktpdvtEKEKIE--ALEQQIKQKIAEALNSSELKEKfeeLEAELAAARE 733
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
126-399 |
7.78e-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: 39.57 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 126 KEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTNKHSQELTAEKEKALQTQVQCQQQHEQQKKE-- 203
Cdd:pfam02463 222 EEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKse 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 204 ---LETLHQRNIHQLQSRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEK 280
Cdd:pfam02463 302 llkLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 281 HINQLQTKVAVLEQEIKDKDQLVlrtKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSlsaeLLKANEIIKKLQGDLK 360
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEE---KEAQLLLELARQLEDLLKEEKKEELEILEEEEES----IELKQGKLTEEKEELE 454
|
250 260 270
....*....|....*....|....*....|....*....
gi 575771867 361 TLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQ 399
Cdd:pfam02463 455 KQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQ 493
|
|
| Sas6_CC |
pfam18594 |
Sas6/XLF/XRCC4 coiled-coil domain; This is a coiled-coil domain found at the C-terminal of ... |
111-136 |
7.99e-03 |
|
Sas6/XLF/XRCC4 coiled-coil domain; This is a coiled-coil domain found at the C-terminal of spindle assembly abnormal protein 6 (Sas6). The highly conserved protein SAS-6 constitutes the center of the cartwheel assembly that scaffolds centrioles early in their biogenesis.Structural analysis of Sas6 show that similar to XLF, and XRCC4 it forms a parallel coiled-coil dimer.
Pssm-ID: 408377 [Multi-domain] Cd Length: 30 Bit Score: 34.18 E-value: 7.99e-03
10 20
....*....|....*....|....*.
gi 575771867 111 DVEIKKFLAGCLKCSKEEKLSLTRSL 136
Cdd:pfam18594 1 DSEVKKYLADCLKSLKEEKQLLEQKL 26
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
112-445 |
8.31e-03 |
|
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: 39.26 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 112 VEIKKFLAGCLKCSKEEKLSLTRSLDDVTRQLHITQETLSE-------KMQELDKLRSEWASHTASLTNK-----HSQEL 179
Cdd:TIGR00606 496 TETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQmemltkdKMDKDEQIRKIKSRHSDELTSLlgyfpNKKQL 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 180 TAEKEKALQTQVQCQQQHEQQKKELETLHQrNIHQLQSRLSELEAANKELTERKYKGDSTvRELKAKLAGVEEELQRAKQ 259
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQ-NKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSK 653
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 260 E--------------VLSLRREN---CTLDTECHEKEKHINQ----LQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKV 318
Cdd:TIGR00606 654 QramlagatavysqfITQLTDENqscCPVCQRVFQTEAELQEfisdLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAP 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 319 ALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKN------TVTIQQEKLLAEKEEMLQKERK 392
Cdd:TIGR00606 734 GRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvTIMERFQMELKDVERKIAQQAA 813
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 575771867 393 ESQDAGQFLRAKE--QEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNE 445
Cdd:TIGR00606 814 KLQGSDLDRTVQQvnQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE 868
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
125-434 |
8.57e-03 |
|
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: 39.33 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 125 SKEEKLSLTRSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTASLTnkhsqeltaEKEKALQTQVQCQQQHEQ----Q 200
Cdd:pfam15921 459 SLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQ---------EKERAIEATNAEITKLRSrvdlK 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 201 KKELETLHQRNIHqLQSRLSELEAANKELTERkykgDSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHE--- 277
Cdd:pfam15921 530 LQELQHLKNEGDH-LRNVQTECEALKLQMAEK----DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDrrl 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 278 -----------KEKHINQLQTKVAVLEQE--------------IKD----KDQL---VLRTKEAFDTIQEQKVALEEN-- 323
Cdd:pfam15921 605 elqefkilkdkKDAKIRELEARVSDLELEkvklvnagserlraVKDikqeRDQLlneVKTSRNELNSLSEDYEVLKRNfr 684
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 324 --GEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGD----LKTLMGKLKlKNTVTIQQEKLLAEKEEMLQKERKESQDA 397
Cdd:pfam15921 685 nkSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSdghaMKVAMGMQK-QITAKRGQIDALQSKIQFLEEAMTNANKE 763
|
330 340 350
....*....|....*....|....*....|....*..
gi 575771867 398 GQFLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEK 434
Cdd:pfam15921 764 KHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQER 800
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
202-435 |
9.76e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.00 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 202 KELETLhQRNIHQLQSRLSELEAANKELTerkykgdSTVRELKAKLAGVEEELQRAKQEVLSLRRENCTLDTECHEKEKH 281
Cdd:pfam01576 798 KQLKKL-QAQMKDLQRELEEARASRDEIL-------AQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADE 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 282 INQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATI---KSLSAELLKANEIIKKLQGD 358
Cdd:pfam01576 870 IASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELaaeRSTSQKSESARQQLERQNKE 949
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575771867 359 LKTLMGKL------KLKNTVTIQQEKLlAEKEEMLQKERKESQDAGQFLRAKEQEVCRLQEQLETTVQKLEESK-QLLKN 431
Cdd:pfam01576 950 LKAKLQEMegtvksKFKSSIAALEAKI-AQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKdQAEKG 1028
|
....
gi 575771867 432 NEKL 435
Cdd:pfam01576 1029 NSRM 1032
|
|
| |
