|
Name |
Accession |
Description |
Interval |
E-value |
| HD_SAS6_N |
cd10142 |
N-terminal head domain found in spindle assembly abnormal protein 6 and similar proteins; ... |
1-117 |
8.70e-52 |
|
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: 174.66 E-value: 8.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 1 MSIELQSvSNPVHRKDLVIRLTDDTDPFFLYNLVISEEDFQSLKFQQGLLVDFLAFPQKFIDLLQQCTQEHAKEIPRFLL 80
Cdd:cd10142 25 VKIEILS-SGSGHKKELRVRLTDETDLFFLYTLELNEEDFQSLKEQQGLLVDFSAFPQKLIDLLELCIKEESKEPPKFLL 103
|
90 100 110
....*....|....*....|....*....|....*..
gi 1034556035 81 QLVSPAailDNSPAFLNVVETNPFKHLTHLSLKLLPG 117
Cdd:cd10142 104 VLVISS---DKGRATLEIVETNPFKHLTHLSLKFLPG 137
|
|
| SAS-6_N |
pfam16531 |
Centriolar protein SAS N-terminal; SAS-6_N is the N-terminal domain of the SAS-6 centriolar ... |
17-114 |
2.86e-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: 108.44 E-value: 2.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 17 LVIRLTDDTDPFFLYNLVISEEDFQSLKFQQGLLVDFLAFPQKFIDLLQQCTQEHAKEIprfllqlvspAAILDNSPAFL 96
Cdd:pfam16531 1 LRIELTDDSDLFFLYILEIDEEDFESLKQEQNLLVDFEDFPQKLIKLLNNCIKEPNLLV----------FLIQDDGTATL 70
|
90
....*....|....*...
gi 1034556035 97 NVVETNPFKHLTHLSLKL 114
Cdd:pfam16531 71 VFIENNEFKNLEHLSLDF 88
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
138-423 |
2.22e-16 |
|
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: 83.18 E-value: 2.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 138 LSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEwashtaaltnkhSQELTNEKEKALQAQVQYQQQHEQQKKDLEIL-- 215
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKE------------LEELEEELEQLRKELEELSRQISALRKDLARLea 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 216 ----HQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVN 291
Cdd:TIGR02168 741 eveqLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 292 QLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLM 371
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1034556035 372 GKLKlkntvtiQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQL 423
Cdd:TIGR02168 901 EELR-------ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
155-455 |
4.76e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 155 RKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEILhQQNIHQLQNRLSELEAAN 234
Cdd:COG1196 219 KEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 235 KDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRT 314
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 315 KEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEK 394
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEE 457
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034556035 395 LQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNE-KLITWLNKELNENQ 455
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGL 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
216-455 |
7.61e-13 |
|
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: 72.01 E-value: 7.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 216 HQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQT 295
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 296 KVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEEN-------GEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLK 368
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEElesleaeLEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 369 TLMGKLK-LKNTVTI---QQEKLLAEKEEKLQK-EQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 443
Cdd:TIGR02168 397 SLNNEIErLEARLERledRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250
....*....|..
gi 1034556035 444 ITWLNKELNENQ 455
Cdd:TIGR02168 477 LDAAERELAQLQ 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
136-443 |
1.84e-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: 70.86 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 136 EKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKHSQEltNEKEKALQAQVQYQQQHEQQKKDLEil 215
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEV--SELEEEIEELQKELYALANEISRLE-- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 216 hqQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVEC-------HEKEK 288
Cdd:TIGR02168 302 --QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELeelesrlEELEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 289 HVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLgkLEATIKSLSAELLKANEIIKKLQGDLK 368
Cdd:TIGR02168 380 QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL--EEAELKELQAELEELEEELEELQEELE 457
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034556035 369 TLMGKLKlkntvtiQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQevckLQEQLEatvKKLEESKQLLKNNEKL 443
Cdd:TIGR02168 458 RLEEALE-------ELREELEEAEQALDAAERELAQLQARLDSLER----LQENLE---GFSEGVKALLKNQSGL 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
209-461 |
2.47e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 209 KKDLEIL-HQQNIHQLQNRLSELEAANKDLTERKykgdSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKE 287
Cdd:COG1196 219 KEELKELeAELLLLKLRELEAELEELEAELEELE----AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 288 KHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDL 367
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 368 KTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWL 447
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
250
....*....|....
gi 1034556035 448 NKELNENQLVRKQD 461
Cdd:COG1196 455 EEEEEALLELLAEL 468
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
136-444 |
7.38e-12 |
|
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: 68.56 E-value: 7.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 136 EKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALT--NKHSQELTNEKEKALqaqvqyqqqheqqKKDLE 213
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEelNKKIKDLGEEEQLRV-------------KEKIG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 214 ILHQQnIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQL 293
Cdd:TIGR02169 298 ELEAE-IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 294 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGK 373
Cdd:TIGR02169 377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK 456
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034556035 374 LKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLrikeqevcklqEQLEATVKKLEESKQLLKNNEKLI 444
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL-----------AEAEAQARASEERVRGGRAVEEVL 516
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
135-453 |
3.54e-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: 66.63 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 135 EEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKL---RNEWASHTAALTNKHSQELT---NEKEKALQAQVQYQQQHEQQ 208
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLrreREKAERYQALLKEKREYEGYellKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 209 KKDLEILHQQnIHQLQNRLSELEAANKDLTER-KYKGDSTIRELKAKLSGVEEELQRT-------KQEVLSLRRENSTLD 280
Cdd:TIGR02169 250 EEELEKLTEE-ISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLersiaekERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 281 VECHEKEKHVNQLQTKvavLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLeatiKSLSAELLKANEII 360
Cdd:TIGR02169 329 AEIDKLLAEIEELERE---IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL----KDYREKLEKLKREI 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 361 KKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNN 440
Cdd:TIGR02169 402 NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
330
....*....|...
gi 1034556035 441 EKLITWLNKELNE 453
Cdd:TIGR02169 482 EKELSKLQRELAE 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
265-453 |
8.16e-11 |
|
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: 65.46 E-value: 8.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 265 TKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEA 344
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 345 TIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLE 424
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
170 180
....*....|....*....|....*....
gi 1034556035 425 ATVKKLEESKQLLKNNEKLITWLNKELNE 453
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
209-434 |
1.97e-10 |
|
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: 64.32 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 209 KKDLEILHQ------QNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVE 282
Cdd:TIGR02169 687 KRELSSLQSelrrieNRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 283 CHEKEKHVNQLQTKVAVLEQEIKDkdqlvlrtkEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKK 362
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSH---------SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034556035 363 LQGDLKTLMGKlklKNTVTIQQEKL---LAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESK 434
Cdd:TIGR02169 838 LQEQRIDLKEQ---IKSIEKEIENLngkKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
134-432 |
2.18e-10 |
|
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: 63.93 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 134 KEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWaSHTAALTNKHSQELTNEKEKaLQAQVQYQQQHEQQKKDLE 213
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI-EQLEQEEEKLKERLEELEED-LSSLEQEIENVKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 214 ilhqQNIHQLQNRLSELEAANKDLtERKYkGDSTIRELKAKLSGVEEELQRTKQEVLSLrrenstldvechekEKHVNQL 293
Cdd:TIGR02169 765 ----ARIEELEEDLHKLEEALNDL-EARL-SHSRIPEIQAELSKLEEEVSRIEARLREI--------------EQKLNRL 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 294 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGK 373
Cdd:TIGR02169 825 TLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034556035 374 LKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQ--EQLEATVKKLEE 432
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELslEDVQAELQRVEE 965
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
245-484 |
2.39e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.46 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 245 DSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDK-DQLVLRTKEAFdtiqe 323
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERrEELGERARALY----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 324 qkvvleengeKNQVQLGKLEATIKSLS-AELLKANEIIKKLQGDLKTLMGKLKlkntvtiQQEKLLAEKEEKLQKEQKEL 402
Cdd:COG3883 97 ----------RSGGSVSYLDVLLGSESfSDFLDRLSALSKIADADADLLEELK-------ADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 403 QDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQDVLGPSTTPPAHSSSNTIRSGI 482
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
..
gi 1034556035 483 SP 484
Cdd:COG3883 240 AA 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
246-451 |
6.13e-09 |
|
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: 58.24 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 246 STIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQK 325
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 326 VVLEENGEK---NQVQLGKLEATIKSLSAE----LLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKE 398
Cdd:COG4942 100 EAQKEELAEllrALYRLGRQPPLALLLSPEdfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034556035 399 QKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKEL 451
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
222-435 |
9.53e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 58.49 E-value: 9.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 222 QLQNRLSELEAANKDLTERkykgdstIRELKAKLSGVEEELQRTKQE--VLSLRRENSTLdvechekEKHVNQLQTKVAV 299
Cdd:COG3206 165 NLELRREEARKALEFLEEQ-------LPELRKELEEAEAALEEFRQKngLVDLSEEAKLL-------LQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 300 LEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQV--QLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK-- 375
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLraQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQqe 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034556035 376 -------LKNTVTI--QQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQ 435
Cdd:COG3206 311 aqrilasLEAELEAlqAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
217-451 |
1.17e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 217 QQNIHQLQNRLSELEAANKDLTERkykgdstIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTK 296
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKE-------LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 297 VAVLEQEIKD-KDQLVLRTKEAFDTIQEQKVVLEENGEkNQVQLGKLEATIKSLSAELlkaNEIIKKLQGDLKTLmgklk 375
Cdd:COG4942 92 IAELRAELEAqKEELAELLRALYRLGRQPPLALLLSPE-DFLDAVRRLQYLKYLAPAR---REQAEELRADLAEL----- 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556035 376 lkNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKEL 451
Cdd:COG4942 163 --AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
222-445 |
3.20e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.00 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 222 QLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQR---TKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVA 298
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 299 VLEQEIKDKDQLVLRTKE------AFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLqgdlKTLMG 372
Cdd:PRK03918 270 ELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL----EELKK 345
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034556035 373 KLKlkntvtiQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLIT 445
Cdd:PRK03918 346 KLK-------ELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKIT 411
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
248-451 |
3.43e-08 |
|
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: 57.00 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 248 IRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDK-------DQLVLRTKEAFDT 320
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELeedlsslEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 321 IQEQKVVLEENGEKNQVQLGKLEAT-----IKSLSAELLKANEIIKKLQGDLKTLMGKLKlkntvtiqqeKLLAEKEEkL 395
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLN----------RLTLEKEY-L 831
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556035 396 QKEQKELQDVGQSLRIKEQEVCKLQEQLEAtvkKLEESKQLLKNNEKLITWLNKEL 451
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNG---KKEELEEELEELEAALRDLESRL 884
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
245-448 |
5.07e-08 |
|
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: 54.16 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 245 DSTIRELKAKLSGVEEELQRTKQEVLSLRREnstldveCHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ 324
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEAR-------LEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 325 KVVleENGEKnqvQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgklklkntvtiqqEKLLAEKEEKLQKEQKELQD 404
Cdd:COG1579 89 KEY--EALQK---EIESLKRRISDLEDEILELMERIEELEEELAEL--------------EAELAELEAELEEKKAELDE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1034556035 405 VGQSLRIKEQEvckLQEQLEATVKKLEEskQLLKNNEKLITWLN 448
Cdd:COG1579 150 ELAELEAELEE---LEAEREELAAKIPP--ELLALYERIRKRKN 188
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
130-453 |
7.82e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 7.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 130 LKCSKEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTN--KHSQELTNEKEKaLQAQVQYQQQHEQ 207
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKleKEVKELEELKEE-IEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 208 QKKDLEILHQQ---NIHQLQNRLSELEAANKDLTERKYKGDSTIR------ELKAKLSGVEEELQRTKQEVLSLRR---E 275
Cdd:PRK03918 253 SKRKLEEKIREleeRIEELKKEIEELEEKVKELKELKEKAEEYIKlsefyeEYLDELREIEKRLSRLEEEINGIEErikE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 276 NSTLDVECHEKEKHVNQLQTKVAVLE------QEIKDK-DQL-VLRTKEAFDTIQEQKVVLEE---NGEKNQVQLGKLEA 344
Cdd:PRK03918 333 LEEKEERLEELKKKLKELEKRLEELEerhelyEEAKAKkEELeRLKKRLTGLTPEKLEKELEElekAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 345 TIKSL---SAELLKANEIIKKLQG------------DLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELqdvgQSL 409
Cdd:PRK03918 413 RIGELkkeIKELKKAIEELKKAKGkcpvcgrelteeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL----EKV 488
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1034556035 410 RIKEQEVCKLQ---EQLEATVKKLEE-SKQLLKNNEKLITWLNKELNE 453
Cdd:PRK03918 489 LKKESELIKLKelaEQLKELEEKLKKyNLEELEKKAEEYEKLKEKLIK 536
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
160-461 |
8.52e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 8.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 160 EKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDleilhqqnIHQLQNRLSELEAA------ 233
Cdd:PRK03918 369 AKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKE--------IKELKKAIEELKKAkgkcpv 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 234 -NKDLTERKYKGdsTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQT--KVAVLEQEIK--DKD 308
Cdd:PRK03918 441 cGRELTEEHRKE--LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEKLKkyNLE 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 309 QLVLRTKEAfdtiqeqkvvleengEKNQVQLGKLEATIKSLSAELLKANEIIKKL----------QGDLKTLMGKLKLKN 378
Cdd:PRK03918 519 ELEKKAEEY---------------EKLKEKLIKLKGEIKSLKKELEKLEELKKKLaelekkldelEEELAELLKELEELG 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 379 TVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVR 458
Cdd:PRK03918 584 FESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE 663
|
...
gi 1034556035 459 KQD 461
Cdd:PRK03918 664 LRE 666
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
223-443 |
1.65e-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: 54.13 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 223 LQNRLSELEAANKDLterkykgdstIRELKAKLSGVEEELQRTKQEVLSLRRENSTLdvechekEKHVNQLQTKVAVLEQ 302
Cdd:pfam07888 32 LQNRLEECLQERAEL----------LQAQEAANRQREKEKERYKRDREQWERQRREL-------ESRVAELKEELRQSRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 303 EIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTI 382
Cdd:pfam07888 95 KHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034556035 383 QQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 443
Cdd:pfam07888 175 QLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
130-453 |
1.67e-07 |
|
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: 54.64 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 130 LKCSKEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEwashTAALTNKHSQELTNEKEKALQAQvqyqqqheqqk 209
Cdd:TIGR04523 255 LNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE----ISDLNNQKEQDWNKELKSELKNQ----------- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 210 kdleilhQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENStldvechEKEKH 289
Cdd:TIGR04523 320 -------EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ-------SYKQE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 290 VNQLQTKVAVLEQEIKDKDQlvlrtkeafdtiqeQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKT 369
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEK--------------LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 370 LMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQ---LEATVKKLEESKQLLKNNEKLitw 446
Cdd:TIGR04523 452 KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEkkeLEEKVKDLTKKISSLKEKIEK--- 528
|
....*..
gi 1034556035 447 LNKELNE 453
Cdd:TIGR04523 529 LESEKKE 535
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
134-463 |
2.42e-07 |
|
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: 53.87 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 134 KEEKLSLMQSLDDATKQLDFTRKTLAEKKQEL----DKLRNEWASHTAALTNKHSQ--ELTNEKEKALQAQVQYQQQHEQ 207
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKSLESQISELKKQNNQLkdniEKKQQEINEKTTEISNTQTQlnQLKDEQNKIKKQLSEKQKELEQ 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 208 QKKDLEILHQQnIHQLQNRLSEL-----EAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVE 282
Cdd:TIGR04523 279 NNKKIKELEKQ-LNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 283 CHEKEKHVNQLQTKVAVLEQEIKDKDQ----LVLRTKEAFDTIQEQKVV---LEENGEKNQVQLGKLEATIKSLSAELLK 355
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLKKENQSYKQeiknLESQINDLESKIQNQEKLnqqKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 356 ANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQE--------------VCKLQE 421
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKElkklneekkeleekVKDLTK 517
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1034556035 422 QLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQDVL 463
Cdd:TIGR04523 518 KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENL 559
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
133-451 |
2.48e-07 |
|
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: 53.87 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 133 SKEEKLSLMQS-LDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAqvqyqqqheqqkkd 211
Cdd:TIGR04523 318 NQEKKLEEIQNqISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYK-------------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 212 leilhqQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVN 291
Cdd:TIGR04523 384 ------QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 292 QLQTKVAVLEQEIKD---------------KDQLVLRTKEaFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKA 356
Cdd:TIGR04523 458 NLDNTRESLETQLKVlsrsinkikqnleqkQKELKSKEKE-LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEK 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 357 NEIIKKLQGDLKTL---MGKLKLKNTVTIQQEKLL-------------AEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQ 420
Cdd:TIGR04523 537 ESKISDLEDELNKDdfeLKKENLEKEIDEKNKEIEelkqtqkslkkkqEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE 616
|
330 340 350
....*....|....*....|....*....|.
gi 1034556035 421 EQLEATVKKLEESKQLLKNNEKLITWLNKEL 451
Cdd:TIGR04523 617 KELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
259-460 |
2.83e-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: 53.92 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 259 EEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDkdqlvlrtkeafdtIQEQKVVLEENGEKNQVQ 338
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE--------------IEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 339 LGKLEATIKSLSAELLKANEIIKKLqgdlktlmgklklkntvtiqqEKLLAEKEEKLQKEQKELQDVGQSLRikeqevck 418
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKEL---------------------EARIEELEEDLHKLEEALNDLEARLS-------- 789
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1034556035 419 lQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 460
Cdd:TIGR02169 790 -HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
248-461 |
3.09e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 248 IRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVV 327
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 328 LEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQ 407
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAE 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034556035 408 SLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQD 461
Cdd:COG4372 207 KLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
294-442 |
3.46e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.91 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 294 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLK----- 368
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGerara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 369 ---------------------TLMGKLKLKNTVTIQQEKLLAE---KEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLE 424
Cdd:COG3883 95 lyrsggsvsyldvllgsesfsDFLDRLSALSKIADADADLLEElkaDKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170
....*....|....*...
gi 1034556035 425 ATVKKLEESKQLLKNNEK 442
Cdd:COG3883 175 AQQAEQEALLAQLSAEEA 192
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
212-455 |
9.99e-07 |
|
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: 52.04 E-value: 9.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 212 LEILHQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEElqrtkqevlsLRRENSTLDVECHEKEKHVN 291
Cdd:pfam15921 258 IELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQ----------ARNQNSMYMRQLSDLESTVS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 292 QLQTKVAVLEQEIKDK-----DQLVLRTKEAFDTIQEQKVVLEENGEKNQvQLGKLEATIKSLSAELLKANEIIKKL--- 363
Cdd:pfam15921 328 QLRSELREAKRMYEDKieeleKQLVLANSELTEARTERDQFSQESGNLDD-QLQKLLADLHKREKELSLEKEQNKRLwdr 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 364 -QGDLKT---LMGKLKLKNTVTIQQEKLL----AEKEEKLQKEQKELQDVGQSLrikeQEVCKLQEQLEAT-------VK 428
Cdd:pfam15921 407 dTGNSITidhLRRELDDRNMEVQRLEALLkamkSECQGQMERQMAAIQGKNESL----EKVSSLTAQLESTkemlrkvVE 482
|
250 260
....*....|....*....|....*..
gi 1034556035 429 KLEESKQLLKNNEKLITWLNKELNENQ 455
Cdd:pfam15921 483 ELTAKKMTLESSERTVSDLTASLQEKE 509
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
158-371 |
1.43e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 158 LAEKKQELDKLRNEWASHTAALtnkhsQELTNEKEKALQAQVQYQQQHEQQKKDLEIL-HQQNIHQLQNRLSELEAANKD 236
Cdd:COG4913 612 LAALEAELAELEEELAEAEERL-----EALEAELDALQERREALQRLAEYSWDEIDVAsAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 237 LterkykgdstiRELKAKLSGVEEELQRTKQEvlslrrenstldvechekekhVNQLQTKVAVLEQEIKDKDQLVLRTKE 316
Cdd:COG4913 687 L-----------AALEEQLEELEAELEELEEE---------------------LDELKGEIGRLEKELEQAEEELDELQD 734
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034556035 317 AFDTIQE-QKVVLEENGEK--NQVQLGKLEATI-KSLSAELLKANEIIKKLQGDLKTLM 371
Cdd:COG4913 735 RLEAAEDlARLELRALLEErfAAALGDAVERELrENLEERIDALRARLNRAEEELERAM 793
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
220-456 |
1.62e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 220 IHQLQNRLSELEAANKDL---TERKYKGDSTIRELKAKLSGVEEELQRTKQEV-LSLRRENSTLDV---ECHEKEKHVNQ 292
Cdd:PRK02224 281 VRDLRERLEELEEERDDLlaeAGLDDADAEAVEARREELEDRDEELRDRLEECrVAAQAHNEEAESlreDADDLEERAEE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 293 LQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMG 372
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARE 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 373 KLKlkntvtiQQEKLLA---------------------EKEEKLQKEQKELQDvgqsLRIKEQEVCKLQEQLEATVK--- 428
Cdd:PRK02224 441 RVE-------EAEALLEagkcpecgqpvegsphvetieEDRERVEELEAELED----LEEEVEEVEERLERAEDLVEaed 509
|
250 260
....*....|....*....|....*...
gi 1034556035 429 KLEESKQLLKNNEKLITWLNKELNENQL 456
Cdd:PRK02224 510 RIERLEERREDLEELIAERRETIEEKRE 537
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
210-461 |
2.89e-06 |
|
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: 50.40 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 210 KDLE---ILHQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDvechEK 286
Cdd:TIGR04523 57 KNLDknlNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLE----KQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 287 EKHVNQLQTKVAVleqEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKAN---EIIKKL 363
Cdd:TIGR04523 133 KKENKKNIDKFLT---EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLElllSNLKKK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 364 QGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 443
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQ 289
|
250
....*....|....*...
gi 1034556035 444 ITWLNKELNENQLVRKQD 461
Cdd:TIGR04523 290 LNQLKSEISDLNNQKEQD 307
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
130-490 |
3.92e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 130 LKCSKEEKL---SLMQSLDDATKQLDFTRKTlAEKKQELDKLRNEWASHTA-----ALTNKHSQEL--TNEKEKALQAQV 199
Cdd:PTZ00121 1475 AKKKAEEAKkadEAKKKAEEAKKKADEAKKA-AEAKKKADEAKKAEEAKKAdeakkAEEAKKADEAkkAEEKKKADELKK 1553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 200 QYQQQHEQQKKDLEILH--QQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEElQRTKQEvlSLRREns 277
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKkaEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAE--ELKKA-- 1628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 278 tldvecHEKEKHVNQLQTKVavlEQEIKDKDQLvlRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKAN 357
Cdd:PTZ00121 1629 ------EEEKKKVEQLKKKE---AEEKKKAEEL--KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE 1697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 358 EIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKqll 437
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR--- 1774
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1034556035 438 KNNEKLItwlNKELNENQLVRKQDVlgPSTTPPAHSSSNTIRSGISPNLNVVD 490
Cdd:PTZ00121 1775 KEKEAVI---EEELDEEDEKRRMEV--DKKIKDIFDNFANIIEGGKEGNLVIN 1822
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
227-447 |
4.66e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 227 LSELEAANKDLteRKYKGDSTIRELKaKLSGVEEELQRTKQEVLSLRRENSTLDvechEKEKHVNQLQTKVAVLEQEIKD 306
Cdd:COG4717 48 LERLEKEADEL--FKPQGRKPELNLK-ELKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 307 KDQLvlrtKEAFDTIQEQKVvLEENGEKNQVQLGKLEA---TIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQ 383
Cdd:COG4717 121 LEKL----LQLLPLYQELEA-LEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034556035 384 QeklLAEKEEKLQKEQKELQdvgQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWL 447
Cdd:COG4717 196 D---LAEELEELQQRLAELE---EELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
134-367 |
4.69e-06 |
|
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: 49.38 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 134 KEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALtnKHSQELTNEKEKALQAQVQYQQQHEQQKKDLE 213
Cdd:COG4942 47 KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI--AELRAELEAQKEELAELLRALYRLGRQPPLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 214 ILHQQNIHQLQNRLSELEAANKDLTERkykgdstIRELKAKLsgveEELQRTKQEVLSLRRenstldvechEKEKHVNQL 293
Cdd:COG4942 125 LLSPEDFLDAVRRLQYLKYLAPARREQ-------AEELRADL----AELAALRAELEAERA----------ELEALLAEL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034556035 294 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANeiIKKLQGDL 367
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG--FAALKGKL 255
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
185-449 |
5.90e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.79 E-value: 5.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 185 QELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQNIHQlQNRLSELEAANKDLTerkykgdSTIRELKAKLSGVEEELQR 264
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEE-KNALQEQLQAETELC-------AEAEEMRARLAARKQELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 265 TKQEvlslrrenstLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEA 344
Cdd:pfam01576 76 ILHE----------LESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 345 TIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLE 424
Cdd:pfam01576 146 QNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA 225
|
250 260
....*....|....*....|....*.
gi 1034556035 425 ATVKKLEESK-QLLKNNEKLITWLNK 449
Cdd:pfam01576 226 ELQAQIAELRaQLAKKEEELQAALAR 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
156-401 |
6.26e-06 |
|
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: 48.99 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 156 KTLAEKKQELDKLRNEwashtAALTNKHSQELTNEKEKALqaqvqyqqqheqqkKDLEILhQQNIHQLQNRLSELEAANK 235
Cdd:COG4942 20 DAAAEAEAELEQLQQE-----IAELEKELAALKKEEKALL--------------KQLAAL-ERRIAALARRIRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 236 DLTERkykgdstIRELKAKLSGVEEELQRTKQE----VLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLV 311
Cdd:COG4942 80 ALEAE-------LAELEKEIAELRAELEAQKEElaelLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 312 LRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKntvtIQQEKLLAEK 391
Cdd:COG4942 153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL----QQEAEELEAL 228
|
250
....*....|
gi 1034556035 392 EEKLQKEQKE 401
Cdd:COG4942 229 IARLEAEAAA 238
|
|
| CAGE1 |
pfam15066 |
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in ... |
212-445 |
6.69e-06 |
|
Cancer-associated gene protein 1 family; CAGE-1 is a family of proteins overexpressed in tumour tissues compared with surrounding tissues. CAGE-1 gene showed testis-specific expression among normal tissues and displayed wide expression in a variety of cancer cell lines and cancer tissues. CAGE-1 is predominantly expressed during post-meiotic stages. It localizes to the acrosomal matrix and acrosomal granule showing it to be a component of the acrosome of mammalian spermatids and spermatozoa.
Pssm-ID: 464481 Cd Length: 528 Bit Score: 49.06 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 212 LEILHQQNiHQLQNRLSELEAANKDLTERkykgdstIRELKAKLsgveeelqrTKQEVLslrrenstLDVechekekhVN 291
Cdd:pfam15066 320 LQKLKHTN-RKQQMQIQDLQCSNLYLEKK-------VKELQMKI---------TKQQVF--------VDI--------IN 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 292 QLQTKVavlEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENgeKNQVQLGKLEATIKSLSAELLKANEIikKLQGDLKTLM 371
Cdd:pfam15066 367 KLKENV---EELIEDKYNVILEKNDINKTLQNLQEILANT--QKHLQESRKEKETLQLELKKIKVNYV--HLQERYITEM 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 372 GKLKLKNTVTIQQEKLLAEKEE---KLQKEQKELQDVGQSL--------RIKEQEVCKLQEQLEATVKK-LEESKQLLKN 439
Cdd:pfam15066 440 QQKNKSVSQCLEMDKTLSKKEEeveRLQQLKGELEKATTSAldllkrekETREQEFLSLQEEFQKHEKEnLEERQKLKSR 519
|
....*.
gi 1034556035 440 NEKLIT 445
Cdd:pfam15066 520 LEKLVA 525
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
159-457 |
7.76e-06 |
|
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: 49.35 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 159 AEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKAlqaqVQYQQQHEQQKKDLEILHQQNIHQ---LQNRLSELEAA-- 233
Cdd:pfam15921 252 SESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKA----SSARSQANSIQSQLEIIQEQARNQnsmYMRQLSDLESTvs 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 234 --NKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLD-------VECHEKEKHVN--QLQTK------ 296
Cdd:pfam15921 328 qlRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDdqlqkllADLHKREKELSleKEQNKrlwdrd 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 297 ------VAVLEQEIKDKDQLVLRTKEAFDTIQ-EQKVVLEENGEKNQVQLGKLEaTIKSLSAELLKANEIIKKLQGDLKT 369
Cdd:pfam15921 408 tgnsitIDHLRRELDDRNMEVQRLEALLKAMKsECQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTA 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 370 LMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQ---EQLEATVKKLEESKQLLKNNEKLITW 446
Cdd:pfam15921 487 KKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKnegDHLRNVQTECEALKLQMAEKDKVIEI 566
|
330
....*....|..
gi 1034556035 447 LNKEL-NENQLV 457
Cdd:pfam15921 567 LRQQIeNMTQLV 578
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
321-432 |
8.26e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 8.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 321 IQEQKVVLEENGEKNQVQLGKLEAtiKSLSAE-LLKANEIIKKLQ----GDLKTLMGKLKLKNTVTIQQEKLLAEKEEKL 395
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEA--EAIKKEaLLEAKEEIHKLRnefeKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110
....*....|....*....|....*....|....*..
gi 1034556035 396 QKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEE 432
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
245-443 |
8.71e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 8.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 245 DSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ 324
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 325 KVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK-LKNTVTIQQEKLLAEKEEKLQKEQKELQ 403
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLEsLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1034556035 404 DVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 443
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA 229
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
233-400 |
8.78e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 233 ANKDLTERKYKGDSTIRELKAKLSGVEEE-LQRTKQEVLSLRREnstLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLV 311
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKEAEAIKKEaLLEAKEEIHKLRNE---FEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 312 LRTKEAFDTiqeqkvvLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGD------LKTLMGKLKLKNTVTIQQe 385
Cdd:PRK12704 106 EKREEELEK-------KEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEeakeilLEKVEEEARHEAAVLIKE- 177
|
170
....*....|....*
gi 1034556035 386 kllAEKEEKLQKEQK 400
Cdd:PRK12704 178 ---IEEEAKEEADKK 189
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
105-460 |
9.88e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 9.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 105 KHLTHLSLKLLPGNDVEIKKFLAGClkcSKEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKHS 184
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKKRLTGL---TPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 185 ------QELTNEKEKALQAQVQYQQQHEqqKKDLEILHQQnIHQLQNRLSELEAANKDLTE--RKYKGDSTIRELKAKLS 256
Cdd:PRK03918 437 kcpvcgRELTEEHRKELLEEYTAELKRI--EKELKEIEEK-ERKLRKELRELEKVLKKESEliKLKELAEQLKELEEKLK 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 257 GV--------EEELQRTKQEVLSLRRENSTLDVECHEK---EKHVNQLQTKVAVLEQEIKD-KDQLVLRTKEAFDTIQEQ 324
Cdd:PRK03918 514 KYnleelekkAEEYEKLKEKLIKLKGEIKSLKKELEKLeelKKKLAELEKKLDELEEELAElLKELEELGFESVEELEER 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 325 KVVLEE-----NGEKNQVQ-LGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKlkntvtiQQEKLLAEKE-EKLQK 397
Cdd:PRK03918 594 LKELEPfyneyLELKDAEKeLEREEKELKKLEEELDKAFEELAETEKRLEELRKELE-------ELEKKYSEEEyEELRE 666
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034556035 398 EQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 460
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
216-455 |
1.03e-05 |
|
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: 48.58 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 216 HQQNI--HQLQNRLSELEAAN-KDLTERKYKGDSTIRELKAKLSGVEEELQR-----TKQEVLSLRRENSTLDVECHEKE 287
Cdd:pfam17380 280 HQKAVseRQQQEKFEKMEQERlRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaiyAEQERMAMERERELERIRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 288 KHVNQL-QTKVAVLEQEIKDKDQLVL-------RTKEAFDTIQEQKVVLEENGEKNQVQLGKLEatikSLSAELLKANEI 359
Cdd:pfam17380 360 RELERIrQEEIAMEISRMRELERLQMerqqkneRVRQELEAARKVKILEEERQRKIQQQKVEME----QIRAEQEEARQR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 360 -IKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQdvgqslriKEQEVCKLQEQLEATV--KKLEESKQL 436
Cdd:pfam17380 436 eVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE--------KEKRDRKRAEEQRRKIleKELEERKQA 507
|
250
....*....|....*....
gi 1034556035 437 LKNNEKLITWLNKELNENQ 455
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQ 526
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
217-421 |
1.06e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 47.88 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 217 QQNIHQLQNRLSELEAANkDLTERKYKGDST---IRELKAKLSGVEEELQRTKQEVLSLRREnstLDVECHEKEKHVNQL 293
Cdd:pfam15905 121 SASVASLEKQLLELTRVN-ELLKAKFSEDGTqkkMSSLSMELMKLRNKLEAKMKEVMAKQEG---MEGKLQVTQKNLEHS 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 294 QTKVAVLEQEIKDKDQLVLRTK----EAFDTIQEQKVVLEEnGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKT 369
Cdd:pfam15905 197 KGKVAQLEEKLVSTEKEKIEEKseteKLLEYITELSCVSEQ-VEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSK 275
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034556035 370 LMGKLKLK-NTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQE 421
Cdd:pfam15905 276 QIKDLNEKcKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
217-429 |
1.84e-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: 47.45 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 217 QQNIHQLQNRLSELEAANKDLTERkykgdstIRELKAKLSGVEEELQRTKQEVLSLRREnstLDVECHEKEKHVNQLQTk 296
Cdd:COG4942 47 KKEEKALLKQLAALERRIAALARR-------IRALEQELAALEAELAELEKEIAELRAE---LEAQKEELAELLRALYR- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 297 vavleQEIKDKDQLVLRTKEAFDTIQEQKvVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKL 376
Cdd:COG4942 116 -----LGRQPPLALLLSPEDFLDAVRRLQ-YLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034556035 377 KNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKK 429
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
133-425 |
2.70e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 133 SKEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAAL--TNKHSQELTNEKEKALQAQVQYQQQHEQQKK 210
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELeqLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 211 DLEILHQQnIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKE--K 288
Cdd:COG4372 109 EAEELQEE-LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAldE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 289 HVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLK 368
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034556035 369 TLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEA 425
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| HD_XRCC4-like_N |
cd22210 |
N-terminal head domain found in the XRCC4 superfamily of proteins; The XRCC4 superfamily ... |
17-117 |
3.40e-05 |
|
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: 43.30 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 17 LVIRLTDDtdpFFLYNLVISEEDFQSLKFQQGLLVDFLAFPQKFIDLLQQCtqehAKEIPR--FLLQLVSPAAILdnspa 94
Cdd:cd22210 28 LRLHVSDD---AFLWTGEVSESDISQLKNDQGILVDFASFPGKLRSALEKC----ILASDRftFVLTIRGDEAYL----- 95
|
90 100
....*....|....*....|...
gi 1034556035 95 flnVVETNPFKHLTHLSLKLLPG 117
Cdd:cd22210 96 ---KLVEILDEQLPHITFALRKV 115
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
218-434 |
3.74e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 218 QNIHQLQNRLSELEAANKDLTERKYKgdstiRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEkhVNQLQTKV 297
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQ-----IELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR--LELLEAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 298 AVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQ-LGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgKLKL 376
Cdd:COG4913 298 EELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrLEQLEREIERLERELEERERRRARLEALLAAL--GLPL 375
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 377 KNTVTI--QQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESK 434
Cdd:COG4913 376 PASAEEfaALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
285-460 |
3.94e-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: 46.30 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 285 EKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQ 364
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 365 GDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLI 444
Cdd:COG4942 104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170
....*....|....*.
gi 1034556035 445 TWLNKELNENQLVRKQ 460
Cdd:COG4942 184 EEERAALEALKAERQK 199
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
226-453 |
4.09e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 226 RLSELEAANKDLTErkykgdsTIRELKAKLSGVEEELQRTkQEVLSLRRENSTldvECHEKEKHVNQLQTKVAVLEQEIK 305
Cdd:PRK03918 156 GLDDYENAYKNLGE-------VIKEIKRRIERLEKFIKRT-ENIEELIKEKEK---ELEEVLREINEISSELPELREELE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 306 DKDQLVLR---TKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQgdlktlmgKLKLKNTVTI 382
Cdd:PRK03918 225 KLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK--------ELKEKAEEYI 296
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034556035 383 QQEKLLAEKEEKLQKEQKELQDVgqslrikEQEVCKLQEQLeatvKKLEESKQLLKNNEKLITWLNKELNE 453
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRL-------EEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEE 356
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
130-460 |
4.35e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 130 LKCSKEEKlslmQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKhSQELTNEKEKALQAQVQYQQQHEQQK 209
Cdd:PTZ00121 1423 AKKKAEEK----KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK-ADEAKKKAEEAKKADEAKKKAEEAKK 1497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 210 KDLEILHQQNIHQLQNRLSELEAANKDLTERKYKGDSTIREL-KAKLSGVEEELQRTKQevlsLRRENSTLDVECHEKEK 288
Cdd:PTZ00121 1498 KADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAkKAEEKKKADELKKAEE----LKKAEEKKKAEEAKKAE 1573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 289 HVNQLQTKVAVLEQEIKDKdqlvlRTKEAFDTIQEQKVVLEENGEKNQvqlgklEATIKslsAELLKANEIIKKLQGDLK 368
Cdd:PTZ00121 1574 EDKNMALRKAEEAKKAEEA-----RIEEVMKLYEEEKKMKAEEAKKAE------EAKIK---AEELKKAEEEKKKVEQLK 1639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 369 TLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQL---EATVKKLEESKQLLKNNEKLIT 445
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALkkeAEEAKKAEELKKKEAEEKKKAE 1719
|
330
....*....|....*
gi 1034556035 446 WLNKELNENQLVRKQ 460
Cdd:PTZ00121 1720 ELKKAEEENKIKAEE 1734
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
222-443 |
6.46e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 222 QLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDV---ECHEKEKHVNQL----Q 294
Cdd:COG1340 47 ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKaggSIDKLRKEIERLewrqQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 295 TKVAVLEQEIkdkdQLVLRTKEAFDTIQEQKVVLEENGEKN---------QVQLGKLEATIKSLSAELLKANEIIKKLQG 365
Cdd:COG1340 127 TEVLSPEEEK----ELVEKIKELEKELEKAKKALEKNEKLKelraelkelRKEAEEIHKKIKELAEEAQELHEEMIELYK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 366 DLKTLMGKL-KLKNTVTIQQEKL--LAEKEEKLQKEQKELQDVGQSLRIKEQEVcKLQEQLEATVKKLEESKQLLKNNEK 442
Cdd:COG1340 203 EADELRKEAdELHKEIVEAQEKAdeLHEEIIELQKELRELRKELKKLRKKQRAL-KREKEKEELEEKAEEIFEKLKKGEK 281
|
.
gi 1034556035 443 L 443
Cdd:COG1340 282 L 282
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
163-463 |
6.64e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 163 QELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEILHQ---QNIHQLQNRLSELEAANKDLTE 239
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLplyQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 240 RKykgdSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTldvechEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFD 319
Cdd:COG4717 154 RL----EELRELEEELEELEAELAELQEELEELLEQLSL------ATEEELQDLAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 320 TIQEQKVVLEENGEKNQV--QLGKLEATIKSLSAeLLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQK 397
Cdd:COG4717 224 ELEEELEQLENELEAAALeeRLKEARLLLLIAAA-LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGK 302
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034556035 398 EQKELQDVGQSLRIKEQEVCKL-----------QEQLEATVKKLEESKQLLKNNEKlitwLNKELNENQLVRKQDVL 463
Cdd:COG4717 303 EAEELQALPALEELEEEELEELlaalglppdlsPEELLELLDRIEELQELLREAEE----LEEELQLEELEQEIAAL 375
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
220-443 |
7.32e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 220 IHQLQNRLSELEaankDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAV 299
Cdd:PRK03918 171 IKEIKRRIERLE----KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 300 LEQEIKDKDQLVLRTKEAFDTIQEQKVVLEEngeknqvqLGKLEATIKSLSaELLKANEIIKKLQGDLKTLMGKLKLKNT 379
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEELKKEIEE--------LEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034556035 380 VTIQQEKLLAEKEEKLQKEQKELQDvgqsLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKL 443
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEE----LKKKLKELEKRLEELEERHELYEEAKAKKEELERL 377
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
210-442 |
7.69e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.60 E-value: 7.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 210 KDLEILHQQN---IHQLQNRLSELEaanKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQevlslrrENSTLDVEchEK 286
Cdd:PRK04778 129 QELLESEEKNreeVEQLKDLYRELR---KSLLANRFSFGPALDELEKQLENLEEEFSQFVE-------LTESGDYV--EA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 287 EKHVNQLQTKVAVLEQEIKDKDQLVLRT-----------KEAFDTIQEQKVVLEENGEKNQV-----QLGKLEATIKSLs 350
Cdd:PRK04778 197 REILDQLEEELAALEQIMEEIPELLKELqtelpdqlqelKAGYRELVEEGYHLDHLDIEKEIqdlkeQIDENLALLEEL- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 351 aELLKANEIIKKLQGDLKTLMGKL----KLKNTVTIQQEKL---LAEKEEKLQKEQKELQDVGQSLRIKEQEVCK---LQ 420
Cdd:PRK04778 276 -DLDEAEEKNEEIQERIDQLYDILerevKARKYVEKNSDTLpdfLEHAKEQNKELKEEIDRVKQSYTLNESELESvrqLE 354
|
250 260
....*....|....*....|..
gi 1034556035 421 EQLEATVKKLEESKQLLKNNEK 442
Cdd:PRK04778 355 KQLESLEKQYDEITERIAEQEI 376
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
211-452 |
1.07e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.39 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 211 DLEILH-QQNIHQLQNRLSELEAANKDLTERKykgdstirelKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKH 289
Cdd:PHA02562 187 DMKIDHiQQQIKTYNKNIEEQRKKNGENIARK----------QNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAA 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 290 VNQLQTKVAVLEQEIK--DKDQLVLRT-------KEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEII 360
Cdd:PHA02562 257 LNKLNTAAAKIKSKIEqfQKVIKMYEKggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQS 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 361 KKLQgDLKTLMGKLKlkntvtiQQEKLLAEKEEKLQKEQKELQDvgqSLRIKEQEVCKLQEQLEATVKKLEESKQ----- 435
Cdd:PHA02562 337 KKLL-ELKNKISTNK-------QSLITLVDKAKKVKAAIEELQA---EFVDNAEELAKLQDELDKIVKTKSELVKekyhr 405
|
250 260
....*....|....*....|....*....
gi 1034556035 436 -----LLKNN-------EKLITWLNKELN 452
Cdd:PHA02562 406 givtdLLKDSgikasiiKKYIPYFNKQIN 434
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
217-459 |
1.13e-04 |
|
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: 45.35 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 217 QQNIHQLQNRLSELEAANKDLTERKYKgdsTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTK 296
Cdd:pfam02463 182 TENLAELIIDLEELKLQELKLKEQAKK---ALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQ 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 297 VAVLEQEIKDKDQLVLRTKEAFDTIQE-QKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMG--- 372
Cdd:pfam02463 259 EIEKEEEKLAQVLKENKEEEKEKKLQEeELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEeie 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 373 -KLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDvgqsLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKEL 451
Cdd:pfam02463 339 eLEKELKELEIKREAEEEEEEELEKLQEKLEQL----EEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELA 414
|
....*...
gi 1034556035 452 NENQLVRK 459
Cdd:pfam02463 415 RQLEDLLK 422
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
215-439 |
1.41e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 215 LHQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEeelqRTKQEVLSLRREnstLDVECHEKEKHVNQLQ 294
Cdd:pfam01576 156 LLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEE----KGRQELEKAKRK---LEGESTDLQEQIAELQ 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 295 TKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKL 374
Cdd:pfam01576 229 AQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTEL 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556035 375 KLKNTVTIQQEKLLAEKEEKLQKEQKELQDVG-------QSLRIKE-QEVCKLQEQLEATVK---KLEESKQLLKN 439
Cdd:pfam01576 309 EDTLDTTAAQQELRSKREQEVTELKKALEEETrsheaqlQEMRQKHtQALEELTEQLEQAKRnkaNLEKAKQALES 384
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
248-444 |
1.88e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 44.71 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 248 IRELKAKLSGVEEELQRtkqEVLSLRRENSTLDVECHEKEkhvNQLQTKVAVLEQEIKDKDQLVLRTK---EAFDTIQEQ 324
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKE---NKMKDLTFLLEESRDKANQLEEKTKlqdENLKELIEK 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 325 KVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNT----VTIQQEKLLAEKEEKLQKEQK 400
Cdd:pfam05483 291 KDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAahsfVVTEFEATTCSLEELLRTEQQ 370
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034556035 401 ELQDVGQSLRIKEQEVCKLQEQLEATVK-------KLEESKQLLKNNEKLI 444
Cdd:pfam05483 371 RLEKNEDQLKIITMELQKKSSELEEMTKfknnkevELEELKKILAEDEKLL 421
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
212-458 |
1.99e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 44.53 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 212 LEILHQQNIHQLQNrLSELEAANKDLTERKYKGD-----STIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEK 286
Cdd:PRK05771 22 LEALHELGVVHIED-LKEELSNERLRKLRSLLTKlsealDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 287 EkhVNQLQTKVAVLEQEIKDKDQLVLRTK--EAFDTiqeqKVVLEENGEKNQVQLGKLEATIKS-LSAELLKANEIIKKl 363
Cdd:PRK05771 101 E--IKELEEEISELENEIKELEQEIERLEpwGNFDL----DLSLLLGFKYVSVFVGTVPEDKLEeLKLESDVENVEYIS- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 364 qgdlktlmgKLKLKNTVTIQQEKLLAEK-EEKLQK---EQKELQDVG---QSLRIKEQEVCKLQEQLEATVKKLEESKQl 436
Cdd:PRK05771 174 ---------TDKGYVYVVVVVLKELSDEvEEELKKlgfERLELEEEGtpsELIREIKEELEEIEKERESLLEELKELAK- 243
|
250 260
....*....|....*....|..
gi 1034556035 437 lKNNEKLITWlnKELNENQLVR 458
Cdd:PRK05771 244 -KYLEELLAL--YEYLEIELER 262
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
154-460 |
2.14e-04 |
|
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: 44.58 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 154 TRKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQNIHQLQNRLSELEAA 233
Cdd:pfam02463 665 KASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQK 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 234 NKDLTERKYKGDSTIRELKAKLSgvEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLR 313
Cdd:pfam02463 745 IDEEEEEEEKSRLKKEEKEEEKS--ELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 314 TKEAFDTIQEQKVVLEENGEKN-QVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNtvTIQQEKLLAEKE 392
Cdd:pfam02463 823 LIEQEEKIKEEELEELALELKEeQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDEL--ESKEEKEKEEKK 900
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034556035 393 EKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQ 460
Cdd:pfam02463 901 ELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLA 968
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
142-543 |
2.26e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 142 QSLDDATKQLDFTRKTLAEKKQELDKLRNEwashtAALTNKHSQELTNEKE---KALQAQVQYQQQHEQQKKDLEILHQQ 218
Cdd:pfam15921 496 RTVSDLTASLQEKERAIEATNAEITKLRSR-----VDLKLQELQHLKNEGDhlrNVQTECEALKLQMAEKDKVIEILRQQ 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 219 --NIHQLQNR--------LSELEAANKDLTER----------KYKGDSTIRELKAKLSGVEeelqrtkqevlslrrenst 278
Cdd:pfam15921 571 ieNMTQLVGQhgrtagamQVEKAQLEKEINDRrlelqefkilKDKKDAKIRELEARVSDLE------------------- 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 279 ldvecHEKEKHVNQLQTKVAVLEQEIKDKDQL---VLRTKEAFDTIQEQKVVLEEN----GEKNQVQLGKLEATIKSLSA 351
Cdd:pfam15921 632 -----LEKVKLVNAGSERLRAVKDIKQERDQLlneVKTSRNELNSLSEDYEVLKRNfrnkSEEMETTTNKLKMQLKSAQS 706
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 352 ELLKANEIIKKLQGD----LKTLMGKLK-----------LKNTVTIQQEKLL-AEKEEKLQKEQKelQDVGQSLRIKEQE 415
Cdd:pfam15921 707 ELEQTRNTLKSMEGSdghaMKVAMGMQKqitakrgqidaLQSKIQFLEEAMTnANKEKHFLKEEK--NKLSQELSTVATE 784
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 416 VCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQ-LVRKQDvlgpsttppahssSNTIRSGISPNLNVVDGRlt 494
Cdd:pfam15921 785 KNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQdIIQRQE-------------QESVRLKLQHTLDVKELQ-- 849
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1034556035 495 yptcGIGYPVSSAFAFQNTFPHSISAKNTSHPGSGTKVQF-NLQFTKPNA 543
Cdd:pfam15921 850 ----GPGYTSNSSMKPRLLQPASFTRTHSNVPSSQSTASFlSHHSRKTNA 895
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
126-432 |
2.32e-04 |
|
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: 44.12 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 126 LAGCLKcskeEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALtNKHSQELTNEKEKALQAQVQYQQQH 205
Cdd:pfam07888 36 LEECLQ----ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAEL-KEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 206 EQQKKDLEILHQQNIHQLQnRLSELEAANKDLTERKYKGDSTIRELK--------------AKLSGVEEELQRTKQEVLS 271
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEA-RIRELEEDIKTLTQRVLERETELERMKerakkagaqrkeeeAERKQLQAKLQQTEEELRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 272 LRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLR---TKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKS 348
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEneaLLEELRSLQERLNASERKVEGLGEELSSMAAQRDR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 349 LSAELLKANEIIKKLQGDLKTLMGKLK------------LKNTVTIQQEKL------LAEKEEKLQKEQ----------- 399
Cdd:pfam07888 270 TQAELHQARLQAAQLTLQLADASLALRegrarwaqeretLQQSAEADKDRIeklsaeLQRLEERLQEERmereklevelg 349
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1034556035 400 --------------KELQDVGQSLRIKEQEvcklQEQLEATVKKLEE 432
Cdd:pfam07888 350 rekdcnrvqlsesrRELQELKASLRVAQKE----KEQLQAEKQELLE 392
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
220-438 |
2.40e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 220 IHQLQN----RLSELEAANKDLTERKYKGDSTirelkaklsGVEEELQRTKQEVLSLRRENSTLDVEchEKEKHVNQLQT 295
Cdd:PRK04778 221 LKELQTelpdQLQELKAGYRELVEEGYHLDHL---------DIEKEIQDLKEQIDENLALLEELDLD--EAEEKNEEIQE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 296 KV----AVLEQEIKDK---DQLVLRTKEAFDTIQEQKVVLEEngEKNQVQLG-----KLEATIKSLSAELlkaNEIIKKL 363
Cdd:PRK04778 290 RIdqlyDILEREVKARkyvEKNSDTLPDFLEHAKEQNKELKE--EIDRVKQSytlneSELESVRQLEKQL---ESLEKQY 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034556035 364 QGDLKTLMGKLKLKNTVTIQQEKLLAEKEEkLQKEQKELQDVGQSLRIKEQEVcklQEQLEATVKKLEESKQLLK 438
Cdd:PRK04778 365 DEITERIAEQEIAYSELQEELEEILKQLEE-IEKEQEKLSEMLQGLRKDELEA---REKLERYRNKLHEIKRYLE 435
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
136-362 |
2.84e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 136 EKLSLMQSLDDATKQLDFTRKTLaekKQELDKLRNEWASHTAALTNKhsqeltnekekalqaqvqyqqqheqqkkdleil 215
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKEL---PAELAELEDELAALEARLEAA--------------------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 216 hQQNIHQLQNRLSELEAANKDLTERkykgdstIRELKAKLSGV--EEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQL 293
Cdd:COG1579 51 -KTELEDLEKEIKRLELEIEEVEAR-------IKKYEEQLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEEL 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034556035 294 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQkvvLEENGEKNQVQLGKLEATIkslSAELLKANEIIKK 362
Cdd:COG1579 123 EEELAELEAELAELEAELEEKKAELDEELAE---LEAELEELEAEREELAAKI---PPELLALYERIRK 185
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
334-453 |
3.24e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 3.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 334 KNQVQLGKLEATIKSLSAELLKANEIIKKLqgdlKTLMGK---LKLKNtvtiQQEKLLAEKEEKLQKEQKELQDVGQSLR 410
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEAEAIKKE----ALLEAKeeiHKLRN----EFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1034556035 411 IKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNE 453
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
185-442 |
3.54e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.56 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 185 QELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQN---IHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLS----- 256
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESrdkANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQrsmst 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 257 --GVEEELQRTKQEVLSLRRENSTLDVECHE-KEKH---VNQLQTKVAVLEQeikdkdqlVLRTkeafdtiQEQKVvlee 330
Cdd:pfam05483 312 qkALEEDLQIATKTICQLTEEKEAQMEELNKaKAAHsfvVTEFEATTCSLEE--------LLRT-------EQQRL---- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 331 ngEKNQVQLGKLEATIKSLSAELLKaneiikklqgdlktlMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLR 410
Cdd:pfam05483 373 --EKNEDQLKIITMELQKKSSELEE---------------MTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELK 435
|
250 260 270
....*....|....*....|....*....|..
gi 1034556035 411 IKEQEVCKLQEQLEATVKKLEESKQLLKNNEK 442
Cdd:pfam05483 436 GKEQELIFLLQAREKEIHDLEIQLTAIKTSEE 467
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
134-437 |
4.39e-04 |
|
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: 43.27 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 134 KEEKLSLMQS-LDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKhsQELTNEKEKALqaqvqyqqqheqqkkdl 212
Cdd:pfam10174 392 KERKINVLQKkIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTL--EEALSEKERII----------------- 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 213 EILHQQNIHQLQNRLSELEAANKDLterkykgdstiRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQ 292
Cdd:pfam10174 453 ERLKEQREREDRERLEELESLKKEN-----------KDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKS 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 293 LqtkvavlEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQvqlgkleaTIKSLSAELLKANEIIKKLQGDLKTLMG 372
Cdd:pfam10174 522 L-------EIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEIND--------RIRLLEQEVARYKEESGKAQAEVERLLG 586
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 373 KLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEV--------------------CKLQEQLEATVKKLEE 432
Cdd:pfam10174 587 ILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMkkkgaqlleearrrednladNSQQLQLEELMGALEK 666
|
....*
gi 1034556035 433 SKQLL 437
Cdd:pfam10174 667 TRQEL 671
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
241-462 |
4.41e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 4.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 241 KYKgdSTIRELKAKLSGVEEELQRtkqevLSLRREnstldvechEKEKHVNQL--QTKVA----VLEQEIKDKDQLVLRT 314
Cdd:COG1196 169 KYK--ERKEEAERKLEATEENLER-----LEDILG---------ELERQLEPLerQAEKAeryrELKEELKELEAELLLL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 315 KeaFDTIQEQKVVLEEngeknqvQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEK 394
Cdd:COG1196 233 K--LRELEAELEELEA-------ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034556035 395 LQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQDV 462
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
148-453 |
5.07e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 148 TKQL-DFTRKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEIlhqqnihQLQNR 226
Cdd:TIGR00606 572 KKQLeDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEES-------DLERL 644
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 227 LSELEAANKDLTERKYKG---DSTIRELKAKLSG----------VEEELQRTKQEVLSLRR----ENSTLDVECHEKEKH 289
Cdd:TIGR00606 645 KEEIEKSSKQRAMLAGATavySQFITQLTDENQSccpvcqrvfqTEAELQEFISDLQSKLRlapdKLKSTESELKKKEKR 724
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 290 VNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSlSAELLKANEIIKKLQGDLKt 369
Cdd:TIGR00606 725 RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEES-AKVCLTDVTIMERFQMELK- 802
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 370 lmgklklkntvtiqqekllaEKEEKLQKEQKELQDVGQSLRIKE--QEVCKLQEQLEATVKKLEESKQLLKNNEKLITWL 447
Cdd:TIGR00606 803 --------------------DVERKIAQQAAKLQGSDLDRTVQQvnQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHL 862
|
....*.
gi 1034556035 448 NKELNE 453
Cdd:TIGR00606 863 KSKTNE 868
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
149-339 |
5.15e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 149 KQLDFTRKTLAEKKQELDKLRNE----WASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDL--------EILH 216
Cdd:COG3206 182 EQLPELRKELEEAEAALEEFRQKnglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgsgpdalpELLQ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 217 QQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVL-SLRRENSTLDVECHEKEKHVNQLQT 295
Cdd:COG3206 262 SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILaSLEAELEALQAREASLQAQLAQLEA 341
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034556035 296 KVAVL---EQEIKDKDQLVLRTKEAFDTIQE--QKVVLEENGEKNQVQL 339
Cdd:COG3206 342 RLAELpelEAELRRLEREVEVARELYESLLQrlEEARLAEALTVGNVRV 390
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
143-409 |
6.81e-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: 42.70 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 143 SLDDATKQLDFTRKTLaekKQELDKLRNEWAShtaaltNKHSQEltnEKEKALQAQVQYQQQHEQQKKDLEilhqQNIHQ 222
Cdd:TIGR04523 451 VKELIIKNLDNTRESL---ETQLKVLSRSINK------IKQNLE---QKQKELKSKEKELKKLNEEKKELE----EKVKD 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 223 LQNRLSELEAANKDLTERKYKGDSTIRELKAKL---------SGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQL 293
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQK 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 294 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEA----------TIKSLSAELLKANEIIKKL 363
Cdd:TIGR04523 595 EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQevkqiketikEIRNKWPEIIKKIKESKTK 674
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556035 364 QGDLKTLMG----------KLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSL 409
Cdd:TIGR04523 675 IDDIIELMKdwlkelslhyKKYITRMIRIKDLPKLEEKYKEIEKELKKLDEFSKEL 730
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
384-455 |
7.22e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 7.22e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034556035 384 QEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQ 455
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
338-453 |
8.66e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 338 QLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKL-----QKE----QKELQDVGQS 408
Cdd:COG1579 25 RLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEyealQKEIESLKRR 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1034556035 409 LRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNE 453
Cdd:COG1579 105 ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
141-456 |
1.20e-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: 42.26 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 141 MQSLDDATKQLDFTRKTLaekKQELDKLRNEwashTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQNI 220
Cdd:TIGR00618 565 MQEIQQSFSILTQCDNRS---KEDIPNLQNI----TVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQC 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 221 HQ-LQNRLSELEAANKDLTERKYKGDS-TIRELKAKLSGV----EEELQRTKQEVLSLRRENSTLDVECHEKEKHV---- 290
Cdd:TIGR00618 638 SQeLALKLTALHALQLTLTQERVREHAlSIRVLPKELLASrqlaLQKMQSEKEQLTYWKEMLAQCQTLLRELETHIeeyd 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 291 -------NQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKL 363
Cdd:TIGR00618 718 refneieNASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREED 797
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 364 QGDLKTLMGKlklkntvtIQQEKLLAEKEEKLQKEQ--KELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNE 441
Cdd:TIGR00618 798 THLLKTLEAE--------IGQEIPSDEDILNLQCETlvQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQA 869
|
330
....*....|....*
gi 1034556035 442 KLITWLNKELNENQL 456
Cdd:TIGR00618 870 KIIQLSDKLNGINQI 884
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
131-435 |
1.35e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 131 KCSKEEKLSLMQSLDDATKQLDFTRKtlAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQ-AQVQYQQQHEQQK 209
Cdd:PTZ00121 1219 KAEDAKKAEAVKKAEEAKKDAEEAKK--AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADElKKAEEKKKADEAK 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 210 KDLEILHQQNIHQLQNRLSELEAANKDLTERKYKGDstirELKAKlsgveEELQRTKQEVLSLRRENSTLDVECHEKEKH 289
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKAD----AAKKK-----AEEAKKAAEAAKAEAEAAADEAEAAEEKAE 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 290 VNQLQTKVAVLE-QEIKDKDQLVLRTKEAFDTIQEQKVVLEE----NGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQ 364
Cdd:PTZ00121 1368 AAEKKKEEAKKKaDAAKKKAEEKKKADEAKKKAEEDKKKADElkkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD 1447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 365 GDLKTLMGKLKLKNTVTIQQEKLLAE----------KEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEA-TVKKLEES 433
Cdd:PTZ00121 1448 EAKKKAEEAKKAEEAKKKAEEAKKADeakkkaeeakKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAeEAKKADEA 1527
|
..
gi 1034556035 434 KQ 435
Cdd:PTZ00121 1528 KK 1529
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
113-469 |
1.37e-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: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 113 KLLPGNDVEIKKFLAGCLKCSKEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEwashtaaltnKHSQELTNEKE 192
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK----------REAQEEQLKKQ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 193 KALQAQVQYQQQHEQQKKDLEilHQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRT------K 266
Cdd:TIGR00618 260 QLLKQLRARIEELRAQEAVLE--ETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRaahvkqQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 267 QEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVlrtkeafdTIQEQKVVLEENGEKNQVQLGKLEATI 346
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIH--------TLQQQKTTLTQKLQSLCKELDILQREQ 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 347 KSLSAELLKANEiikkLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQ---EQL 423
Cdd:TIGR00618 410 ATIDTRTSAFRD----LQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEqihLQE 485
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1034556035 424 EATVKKLEESKQLLKNNEKLITwlNKELNENQLVRKQDVLGPSTTP 469
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLC--GSCIHPNPARQDIDNPGPLTRR 529
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
220-439 |
1.47e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.38 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 220 IHQLQN----RLSELEAANKDLTERKYKGDSTirELKAKLSGVEEELQRTKQEVLSLRRENSTLDVEchEKEKHVNQLQt 295
Cdd:pfam06160 202 YEELKTelpdQLEELKEGYREMEEEGYALEHL--NVDKEIQQLEEQLEENLALLENLELDEAEEALE--EIEERIDQLY- 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 296 kvAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEK-NQVQL-----GKLEATIKSLSAELlkaNEIIKKLQGDLKT 369
Cdd:pfam06160 277 --DLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEElERVQQsytlnENELERVRGLEKQL---EELEKRYDEIVER 351
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 370 LMGKLKLKNTVTIQQEKLLaEKEEKLQKEQKELQDVGQSLRIKEQEVcklQEQLEATVKKLEESKQLLKN 439
Cdd:pfam06160 352 LEEKEVAYSELQEELEEIL-EQLEEIEEEQEEFKESLQSLRKDELEA---REKLDEFKLELREIKRLVEK 417
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
135-445 |
1.58e-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: 41.65 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 135 EEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWAshtaaltnkhsqELTNEKEKALQAQVQYQQQHEQQKKDLEI 214
Cdd:pfam05557 76 ELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELS------------ELRRQIQRAELELQSTNSELEELQERLDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 215 LHQqNIHQLQNRLSELEAANKDLTERKYKgdstIRELKAKLSGVE---EELQRTKQEVLSLRRENSTLDvECHEKEKHVN 291
Cdd:pfam05557 144 LKA-KASEAEQLRQNLEKQQSSLAEAEQR----IKELEFEIQSQEqdsEIVKNSKSELARIPELEKELE-RLREHNKHLN 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 292 QLQTKVAVLEQEIKDkdqlvLRTK-EAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLK----ANEIIKKLQGD 366
Cdd:pfam05557 218 ENIENKLLLKEEVED-----LKRKlEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSpedlSRRIEQLQQRE 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034556035 367 LkTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLIT 445
Cdd:pfam05557 293 I-VLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAILESYDKELT 370
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
226-470 |
1.69e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 226 RLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRR-ENSTLDVECHEKEKHVnqlQTKVAVLEQEI 304
Cdd:PRK05771 80 SVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEPwGNFDLDLSLLLGFKYV---SVFVGTVPEDK 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 305 KDKDQLVLrtkeafdtiqEQKVVLEENGEKNQVQLgkLEATIKSLSAELlkaNEIIKKLQGDlktlmgKLKLKNTVTIQQ 384
Cdd:PRK05771 157 LEELKLES----------DVENVEYISTDKGYVYV--VVVVLKELSDEV---EEELKKLGFE------RLELEEEGTPSE 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 385 ekLLAEKEEKLQKEQKELQDVGQSLR----IKEQEVCKLQEQLEATVKKLEESKQLL--------------KNNEKLITW 446
Cdd:PRK05771 216 --LIREIKEELEEIEKERESLLEELKelakKYLEELLALYEYLEIELERAEALSKFLktdktfaiegwvpeDRVKKLKEL 293
|
250 260
....*....|....*....|....
gi 1034556035 447 LNKELNENQLVRKQDVLGPSTTPP 470
Cdd:PRK05771 294 IDKATGGSAYVEFVEPDEEEEEVP 317
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
134-285 |
1.79e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 134 KEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASH-TAALtnkhsQELTNEKEKALQAQVQYQQQHEQQKKDL 212
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRL-----EQLEREIERLERELEERERRRARLEALL 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556035 213 EILHQQ---NIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHE 285
Cdd:COG4913 369 AALGLPlpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA 444
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
240-453 |
1.83e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 240 RKYKGD--STIRELKAKLsgVEEELQRTKQEVLSLRRENSTLD--VECHEKEKHVNQLQTKVAVLeqeikdkdQLVLRTK 315
Cdd:COG5022 809 RKEYRSylACIIKLQKTI--KREKKLRETEEVEFSLKAEVLIQkfGRSLKAKKRFSLLKKETIYL--------QSAQRVE 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 316 EAFDTIQEQKvvlEENGEKNQVqlgkleatiKSLSAELLK-ANEIIKKLQGDLktlMGKLKLKNTVTIQQEKLLAEKEEK 394
Cdd:COG5022 879 LAERQLQELK---IDVKSISSL---------KLVNLELESeIIELKKSLSSDL---IENLEFKTELIARLKKLLNNIDLE 943
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034556035 395 LQKE-QKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESK-QLLKNNEKLITWlNKELNE 453
Cdd:COG5022 944 EGPSiEYVKLPELNKLHEVESKLKETSEEYEDLLKKSTILVrEGNKANSELKNF-KKELAE 1003
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
130-461 |
1.92e-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: 41.57 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 130 LKCSKEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKHsqELTNEkekaLQAQVQYQQQHEQQK 209
Cdd:TIGR00606 212 LKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIM--KLDNE----IKALKSRKKQMEKDN 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 210 KDLEILHQQNIHQLQNRLSELEAANKdlterkykgdSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVEchekekh 289
Cdd:TIGR00606 286 SELELKMEKVFQGTDEQLNDLYHNHQ----------RTVREKERELVDCQRELEKLNKERRLLNQEKTELLVE------- 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 290 VNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLgkleaTIKSLSAELLKANEIIKKLQGDLKT 369
Cdd:TIGR00606 349 QGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTL-----VIERQEDEAKTAAQLCADLQSKERL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 370 LMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDV---GQSLRIKEQEVCKLQEQL---EATVKKLEESKQLLKNNEKL 443
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVikeLQQLEGSSDRILELDQELrkaERELSKAEKNSLTETLKKEV 503
|
330
....*....|....*...
gi 1034556035 444 ITWLNKELNENQLVRKQD 461
Cdd:TIGR00606 504 KSLQNEKADLDRKLRKLD 521
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
312-458 |
2.12e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.85 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 312 LRTKEAFDTIQEqkVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgklklkntvtIQQEKLLAEK 391
Cdd:PRK12705 30 RLAKEAERILQE--AQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERL-----------VQKEEQLDAR 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034556035 392 EEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEAtvkKLEESKQLLKN--NEKLITWLNKELNENQLVR 458
Cdd:PRK12705 97 AEKLDNLENQLEEREKALSARELELEELEKQLDN---ELYRVAGLTPEqaRKLLLKLLDAELEEEKAQR 162
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
209-453 |
2.30e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 209 KKDLEILHQQNIHQLQNRLSELEAANKDLTERKYKgDSTIRELKAKLSGVEEELQRTKQEVLSLRREN--------STLD 280
Cdd:PRK01156 503 KKRKEYLESEEINKSINEYNKIESARADLEDIKIK-INELKDKHDKYEEIKNRYKSLKLEDLDSKRTSwlnalaviSLID 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 281 VEC-----HEKEKHVNQLQTKVAVLEQEIKD----KDQLVLRTKEAFDTIQEQKVVLEENgeknQVQLGKLEATIKSLSA 351
Cdd:PRK01156 582 IETnrsrsNEIKKQLNDLESRLQEIEIGFPDdksyIDKSIREIENEANNLNNKYNEIQEN----KILIEKLRGKIDNYKK 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 352 ELLKANEIIKKlqgdlktlmgklklKNTVTIQqeklLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQ---EQLEATVK 428
Cdd:PRK01156 658 QIAEIDSIIPD--------------LKEITSR----INDIEDNLKKSRKALDDAKANRARLESTIEILRtriNELSDRIN 719
|
250 260
....*....|....*....|....*
gi 1034556035 429 KLEESKQLLKNNEKLITWLnKELNE 453
Cdd:PRK01156 720 DINETLESMKKIKKAIGDL-KRLRE 743
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
217-465 |
2.47e-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: 41.19 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 217 QQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTK 296
Cdd:TIGR00606 856 QEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETS 935
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 297 VAVLEQEIKDK----DQLVLRTKEAFDTIQEQKvvleengeknQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMG 372
Cdd:TIGR00606 936 NKKAQDKVNDIkekvKNIHGYMKDIENKIQDGK----------DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQ 1005
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 373 KLKLKNtvtiQQEKLLAEkEEKLQKEQKELQDVGQSLRIKEQEVCKLQ-EQLEATVKKLEESKQLLKNNEKLITWLNKEL 451
Cdd:TIGR00606 1006 DIDTQK----IQERWLQD-NLTLRKRENELKEVEEELKQHLKEMGQMQvLQMKQEHQKLEENIDLIKRNHVLALGRQKGY 1080
|
250
....*....|....
gi 1034556035 452 NENQLVRKQDVLGP 465
Cdd:TIGR00606 1081 EKEIKHFKKELREP 1094
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
388-455 |
2.61e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 2.61e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034556035 388 LAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQ 455
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
217-395 |
2.74e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 39.50 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 217 QQNIHQLQNRLSELEAANKDLTERKYKGDSTIR-------ELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKH 289
Cdd:pfam15619 17 QNELAELQSKLEELRKENRLLKRLQKRQEKALGkyegtesELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 290 VNQLQTKVAVLEQEIKDKDqlVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKT 369
Cdd:pfam15619 97 LLRLRDQLKRLEKLSEDKN--LAEREELQKKLEQLEAKLEDKDEKIQDLERKLELENKSFRRQLAAEKKKHKEAQEEVKI 174
|
170 180
....*....|....*....|....*.
gi 1034556035 370 LMGKLKLKNTvtiqqekLLAEKEEKL 395
Cdd:pfam15619 175 LQEEIERLQQ-------KLKEKEREL 193
|
|
| Sas6_CC |
pfam18594 |
Sas6/XLF/XRCC4 coiled-coil domain; This is a coiled-coil domain found at the C-terminal of ... |
119-144 |
2.92e-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: 35.72 E-value: 2.92e-03
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
216-415 |
3.14e-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: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 216 HQQNIHQLQNRLSELEAANKDLteRKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKH------ 289
Cdd:COG4913 260 LAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQirgngg 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 290 --VNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQ----LGKLEATIKSLSAELLKANEIIKKL 363
Cdd:COG4913 338 drLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEaaalLEALEEELEALEEALAEAEAALRDL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556035 364 QGDLKTLMGKLKL----KNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQE 415
Cdd:COG4913 418 RRELRELEAEIASlerrKSNIPARLLALRDALAEALGLDEAELPFVGELIEVRPEE 473
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
349-455 |
3.47e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.13 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 349 LSAELLKANEIIKKLQGDLKTLmgklklkntvtiQQEklLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVK 428
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQL------------QQE--IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ 76
|
90 100
....*....|....*....|....*..
gi 1034556035 429 KLEESKQLLKNNEKLITWLNKELNENQ 455
Cdd:COG4942 77 ELAALEAELAELEKEIAELRAELEAQK 103
|
|
| TOP4c |
cd00187 |
DNA Topoisomerase, subtype IIA; domain A'; bacterial DNA topoisomerase IV (C subunit, ParC), ... |
333-453 |
3.73e-03 |
|
DNA Topoisomerase, subtype IIA; domain A'; bacterial DNA topoisomerase IV (C subunit, ParC), bacterial DNA gyrases (A subunit, GyrA),mammalian DNA toposiomerases II. DNA topoisomerases are essential enzymes that regulate the conformational changes in DNA topology by catalysing the concerted breakage and rejoining of DNA strands during normal cellular growth.
Pssm-ID: 238111 [Multi-domain] Cd Length: 445 Bit Score: 40.24 E-value: 3.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 333 EKNQVQLGKLEATIKSLSAeLLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKElqdvgqslrik 412
Cdd:cd00187 341 GKAEARLHILEGLLKAILN-IDEVINLIRSSDEAKKALIEELEKLGFSEIQADAILDMRLRRLTKLERE----------- 408
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1034556035 413 eqevcKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNE 453
Cdd:cd00187 409 -----KLLKELKELEAEIEDLEKILASEERPKDLWKEELDE 444
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
134-351 |
3.86e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 134 KEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWAShtaaltnkhSQELTNEKEKALQAQVQYQQQHEQQKKDLE 213
Cdd:COG3883 36 QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE---------AEAEIEERREELGERARALYRSGGSVSYLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 214 -ILHQQNIHQLQNR---LSELEAANKDLTErkykgdsTIRELKAKLSGVEEELQRTKQEVLSLRREnstldvechekekh 289
Cdd:COG3883 107 vLLGSESFSDFLDRlsaLSKIADADADLLE-------ELKADKAELEAKKAELEAKLAELEALKAE-------------- 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034556035 290 vnqLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSA 351
Cdd:COG3883 166 ---LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
332-463 |
4.02e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 332 GEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLL--AEKEEKLQKEQKELQDVGQSl 409
Cdd:COG4913 605 GFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDAS- 683
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034556035 410 rikEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELN--ENQLVRKQDVL 463
Cdd:COG4913 684 ---SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEqaEEELDELQDRL 736
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
215-451 |
4.07e-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: 40.11 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 215 LHQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQ 294
Cdd:pfam05557 80 LKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 295 TK---VAVLEQEIKD---------KDQLVLRTKEA---------------------FDTIQEQKVVLEENGEKNQVQLGK 341
Cdd:pfam05557 160 KQqssLAEAEQRIKElefeiqsqeQDSEIVKNSKSelaripelekelerlrehnkhLNENIENKLLLKEEVEDLKRKLER 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 342 LEATIKSLSAELLKANEIIKKLQGDLKTLMgklklKNTVTIQQEKLLAEKEEKLQKEQKELQ----DVGQSLRIKEQEVC 417
Cdd:pfam05557 240 EEKYREEAATLELEKEKLEQELQSWVKLAQ-----DTGLNLRSPEDLSRRIEQLQQREIVLKeensSLTSSARQLEKARR 314
|
250 260 270
....*....|....*....|....*....|....
gi 1034556035 418 KLQEQLEATVKKLEESKQLLKNNEKLITWLNKEL 451
Cdd:pfam05557 315 ELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRV 348
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
130-297 |
4.67e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.05 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 130 LKCSKEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHtaaltNKHSQELTNEKEKAlqaqvqyqqqheqqK 209
Cdd:TIGR02169 359 YAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL-----KRELDRLQEELQRL--------------S 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 210 KDLEILHQQnIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKH 289
Cdd:TIGR02169 420 EELADLNAA-IAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQ 498
|
....*...
gi 1034556035 290 VNQLQTKV 297
Cdd:TIGR02169 499 ARASEERV 506
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
220-451 |
6.11e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 39.17 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 220 IHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENS-------TLDVECHEKEKHVNQ 292
Cdd:pfam09728 6 LMQLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSkailaksKLEKLCRELQKQNKK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 293 LQTKVAVLEQEIKDKDQLVlrtKEAF-DTIQEQKVVLEENGEKNQVQLG---KLEATIKSLSAELLKANEIIKKL--QGD 366
Cdd:pfam09728 86 LKEESKKLAKEEEEKRKEL---SEKFqSTLKDIQDKMEEKSEKNNKLREeneELREKLKSLIEQYELRELHFEKLlkTKE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 367 LKTLMGKLKLKNTvTIQQEKLLAEKEeklQKEQKELQDvgQSLRIKEQEVcKLQEQLEATVKKLEESKQLLKNNEKLITW 446
Cdd:pfam09728 163 LEVQLAEAKLQQA-TEEEEKKAQEKE---VAKARELKA--QVQTLSETEK-ELREQLNLYVEKFEEFQDTLNKSNEVFTT 235
|
....*
gi 1034556035 447 LNKEL 451
Cdd:pfam09728 236 FKKEM 240
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
235-453 |
6.31e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 235 KDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEikdKDQLVLRT 314
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEE---RDELNEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 315 KEAFDTIQEQKVVLEENGEKN------QVQLGKLEATI--KSLSAEllKANEIIKKLQgDLKTLMGKLKlkntVTIQQEK 386
Cdd:COG1340 88 NELREELDELRKELAELNKAGgsidklRKEIERLEWRQqtEVLSPE--EEKELVEKIK-ELEKELEKAK----KALEKNE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034556035 387 LLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNE 453
Cdd:COG1340 161 KLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADE 227
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
222-460 |
9.46e-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: 39.05 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 222 QLQNRL-SELEAANKDLTERKYKGDSTIRELKAKLSGV---EEELQRTKQEVLSLRRENSTLDvechEKEKHVNQLQTKV 297
Cdd:pfam12128 419 ALESELrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQAtatPELLLQLENFDERIERAREEQE----AANAEVERLQSEL 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 298 AVLEqeiKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKL------------EATIKSLSAELLKAN----EIIK 361
Cdd:pfam12128 495 RQAR---KRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLlhflrkeapdweQSIGKVISPELLHRTdldpEVWD 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034556035 362 KLQGDLKTLMG-KLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNN 440
Cdd:pfam12128 572 GSVGGELNLYGvKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNA 651
|
250 260
....*....|....*....|.
gi 1034556035 441 -EKLITWLNKELNENQLVRKQ 460
Cdd:pfam12128 652 rLDLRRLFDEKQSEKDKKNKA 672
|
|
| |
