|
Name |
Accession |
Description |
Interval |
E-value |
| HD_SAS6_N |
cd10142 |
N-terminal head domain found in spindle assembly abnormal protein 6 and similar proteins; ... |
4-144 |
1.68e-58 |
|
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: 192.38 E-value: 1.68e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 4 VLFQQLVPLLVKCKDCEERRGSVRVSIELQSlSNPVHRKDLVIRLTDDTDPFFLYNLVISEEDFQSLKLQQGLLVDFLSF 83
Cdd:cd10142 1 VLYSRELPVEVKSQDREERLEVLRVKIEILS-SGSGHKKELRVRLTDETDLFFLYTLELNEEDFQSLKEQQGLLVDFSAF 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564338581 84 PQKFIDLLQQCMQEHVKETPRFLLQLTSSAallDNSPVFLNVVETNPFKHLIHLSLKLLPG 144
Cdd:cd10142 80 PQKLIDLLELCIKEESKEPPKFLLVLVISS---DKGRATLEIVETNPFKHLTHLSLKFLPG 137
|
|
| SAS-6_N |
pfam16531 |
Centriolar protein SAS N-terminal; SAS-6_N is the N-terminal domain of the SAS-6 centriolar ... |
44-141 |
8.08e-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: 106.89 E-value: 8.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 44 LVIRLTDDTDPFFLYNLVISEEDFQSLKLQQGLLVDFLSFPQKFIDLLQQCMQEhvketprfllQLTSSAALLDNSPVFL 123
Cdd:pfam16531 1 LRIELTDDSDLFFLYILEIDEEDFESLKQEQNLLVDFEDFPQKLIKLLNNCIKE----------PNLLVFLIQDDGTATL 70
|
90
....*....|....*...
gi 564338581 124 NVVETNPFKHLIHLSLKL 141
Cdd:pfam16531 71 VFIENNEFKNLEHLSLDF 88
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
165-464 |
9.54e-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: 81.26 E-value: 9.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 165 LSLTKSLDDVTRQLHITQETLSEKMQELDKLRSEwashtaaltnkhSQELTNEKEKALQTQVQYQQQHEQQKKDLEALHQ 244
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKE------------LEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 245 R------NIHQLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKEKHIN 318
Cdd:TIGR02168 741 EveqleeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 319 QLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLM 398
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564338581 399 GKLKlkntvtiqqekllaEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLL 464
Cdd:TIGR02168 901 EELR--------------ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT 952
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
184-484 |
6.34e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.44 E-value: 6.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 184 TLSEKMQELDK----LRSEWASHTAALTNKHSQELTNEKEKALQTQVQYQQQHEQQKKDLEALHQRnIHQLQNRLSELEA 259
Cdd:COG1196 217 ELKEELKELEAelllLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 260 ANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVL 339
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 340 RTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKE 419
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564338581 420 EMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNE-KLITWLNKELNENQLG 484
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLAGLRG 521
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
171-480 |
2.69e-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: 70.10 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 171 LDDVTRQLHITQETLSEKMQELDKLRSEWAS---HTAALTNKHSQELT---NEKEKALQTQVQYQQQHEQQKKDLEALhQ 244
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLRREREKaerYQALLKEKREYEGYellKEKEALERQKEAIERQLASLEEELEKL-T 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 245 RNIHQLQNRLSELEAANKELTER-KYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKEKHINQLQTK 323
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 324 VAVLEQEI----KDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLeatiKSLSAELLKANEIIKKLQGDLKTLMG 399
Cdd:TIGR02169 338 IEELEREIeeerKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL----KDYREKLEKLKREINELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 400 KLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELN 479
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
.
gi 564338581 480 E 480
Cdd:TIGR02169 494 E 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
237-482 |
1.53e-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: 67.77 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 237 KDLEALHQRnIHQLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKEKH 316
Cdd:TIGR02168 232 LRLEELREE-LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 317 INQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQK-------VALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKK 389
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLeelkeelESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 390 LQGDLKTLMGKLK-LKNTVTI---QQEKLLAEKEEMLQK-ERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLL 464
Cdd:TIGR02168 391 LELQIASLNNEIErLEARLERledRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
250
....*....|....*...
gi 564338581 465 KNNEKLITWLNKELNENQ 482
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQ 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
236-495 |
5.62e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 5.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 236 KKDLEAL-HQRNIHQLQNRLSELEAANKELTERKykgdSTVRELKAKLAGVEEELQRTKQEVLSLRRENctldtecHEKE 314
Cdd:COG1196 219 KEELKELeAELLLLKLRELEAELEELEAELEELE----AELEELEAELAELEAELEELRLELEELELEL-------EEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 315 KHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEEngeknqiQLGKLEATIKSLSAELLKANEIIKKLQGDL 394
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE-------ELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 395 KTLMGKLKLKNTVTIQ-QEKLLAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITW 473
Cdd:COG1196 361 AEAEEALLEAEAELAEaEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250 260
....*....|....*....|..
gi 564338581 474 LNKELNENQLGRKQDTLGASAT 495
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALL 462
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
161-470 |
3.52e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 3.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 161 KEEKLSLTKSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTAALtnkhsQELTNEKEKAlqtqvqyqqqheqqkkdle 240
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKEL-----YALANEISRL------------------- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 241 alhQRNIHQLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTEC-------HEK 313
Cdd:TIGR02168 301 ---EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELeelesrlEEL 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 314 EKHINQLQTKVAVLEQEIKdkdQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKL-EATIKSLSAELLKANEIIKKLQG 392
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIA---SLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELEELQE 454
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564338581 393 DLKTLMGKLKlkntvtiQQEKLLAEKEEMLQKERKESQDAGQSLRAKEqevcRLQEQLETtvqKLEESKQLLKNNEKL 470
Cdd:TIGR02168 455 ELERLEEALE-------ELREELEEAEQALDAAERELAQLQARLDSLE----RLQENLEG---FSEGVKALLKNQSGL 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-441 |
8.84e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 8.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 161 KEEKLSLTKSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTAALTNKHSQELTNEKEKALqtqvqyqqqheqQKKDLE 240
Cdd:COG1196 245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR------------LEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 241 ALhQRNIHQLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENctldtecHEKEKHINQL 320
Cdd:COG1196 313 EL-EERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-------AEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 321 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGK 400
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 564338581 401 LKLKNTVTIQQEKLLAEKEEMLQkERKESQDAGQSLRAKEQ 441
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELA-EAAARLLLLLEAEADYE 504
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
157-480 |
9.25e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.57 E-value: 9.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 157 LKCSKEEKLSLTKSLDDVTRQLHITQETLSEKMQELDKLrsewashTAALTNKHSQ--ELTNEKEKALQTQVQYQQQHEQ 234
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEK-------TTEISNTQTQlnQLKDEQNKIKKQLSEKQKELEQ 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 235 QKKDLEALhQRNIHQLQNRLSEL-----EAANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTE 309
Cdd:TIGR04523 279 NNKKIKEL-EKQLNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 310 CHEKEKHINQLQTKVAVLEQEIKDKDQ----LVLRTKEAFDTIQEQKVA---LEENGEKNQIQLGKLEATIKSLSAELLK 382
Cdd:TIGR04523 358 NSEKQRELEEKQNEIEKLKKENQSYKQeiknLESQINDLESKIQNQEKLnqqKDEQIKKLQQEKELLEKEIERLKETIIK 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 383 ANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQ---LETTVQKLEE 459
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEkkeLEEKVKDLTK 517
|
330 340
....*....|....*....|.
gi 564338581 460 SKQLLKNNEKLitwLNKELNE 480
Cdd:TIGR04523 518 KISSLKEKIEK---LESEKKE 535
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
236-461 |
1.06e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 236 KKDLEALHQR------NIHQLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTE 309
Cdd:TIGR02169 687 KRELSSLQSElrrienRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 310 CHEKEKHINQLQTKVAVLEQEIKDkdqlvlrtkEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKK 389
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSH---------SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564338581 390 LQGDLKTLMGKlklKNTVTIQQEKLLAEKEEMLQKErKESQDAGQSLRAK----EQEVCRLQEQLETTVQKLEESK 461
Cdd:TIGR02169 838 LQEQRIDLKEQ---IKSIEKEIENLNGKKEELEEEL-EELEAALRDLESRlgdlKKERDELEAQLRELERKIEELE 909
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
307-620 |
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 564338581 307 DTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELlkaNEI 386
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL---GER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 387 IKKLQ---------------GDLKTLMGKLKLKNTVTIQQEKLLAE---KEEMLQKERKESQDAGQSLRAKEQEVCRLQE 448
Cdd:COG3883 92 ARALYrsggsvsyldvllgsESFSDFLDRLSALSKIADADADLLEElkaDKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 449 QLETTVQKLEESKQLLKNNEKLITWLNKELnENQLGRKQDTLGASATPPTHSASNTVRSGLSPSLNVVDSRLNYPSCGIG 528
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAEL-EAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 529 YPVSSAFTFQNAFPHAVVAKNTSHPVSGPKVQFSLQLTKQSTSSGDGQPGAAVNRSASADKEKPSERWHAGSAADIFQTH 608
Cdd:COG3883 251 AAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGG 330
|
330
....*....|..
gi 564338581 609 SPAPIFIVFSWA 620
Cdd:COG3883 331 GGGSGGGGGSSG 342
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
272-587 |
4.40e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 58.69 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 272 DSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVlrtkeafdtiQEQ 351
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL----------GER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 352 KVALEENGEknqiQLGKLEATIKSLS-AELLKANEIIKKLQGDLKTLMGKLK-LKNTVTIQQEKLLAEKEEM--LQKERK 427
Cdd:COG3883 92 ARALYRSGG----SVSYLDVLLGSESfSDFLDRLSALSKIADADADLLEELKaDKAELEAKKAELEAKLAELeaLKAELE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 428 ESQDAGQSLRA-KEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLGRKQDTLGASATPPTHSASNTVR 506
Cdd:COG3883 168 AAKAELEAQQAeQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 507 SGLSPSLNVVDSRLNYPSCGIGYPVSSAFTFQNAFPHAVVAKNTSHPVSGPKVQFSLQLTKQSTSSGDGQPGAAVNRSAS 586
Cdd:COG3883 248 GAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGAS 327
|
.
gi 564338581 587 A 587
Cdd:COG3883 328 A 328
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
276-493 |
6.82e-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: 6.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 276 RELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVAL 355
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 356 EENGEK--NQIQLGKLEATIKSL-----SAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKE 428
Cdd:COG4942 103 KEELAEllRALYRLGRQPPLALLlspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564338581 429 SQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLGRKQDTLGAS 493
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
249-478 |
7.19e-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: 7.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 249 QLQNRLSELEAANKELTERKYKgdstVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLE 328
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKE----LAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 329 QEIKDKDQLvlrtkeafdtIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVT 408
Cdd:COG4942 97 AELEAQKEE----------LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 409 IQQEKLLAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKEL 478
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
160-488 |
1.01e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 160 SKEEKLS-LTKSLDDVTRQL------HITQETLSEKMQELDKLRSEWASHTAALTNKHSQELTNEKEKalqtqvqyqqqh 232
Cdd:PRK03918 335 EKEERLEeLKKKLKELEKRLeeleerHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE------------ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 233 eqQKKDLEALHQRnIHQLQNRLSELEAANKELTERKYKGDSTVREL------------KAKLAGVEEELQRTKQEVLSLR 300
Cdd:PRK03918 403 --IEEEISKITAR-IGELKKEIKELKKAIEELKKAKGKCPVCGRELteehrkelleeyTAELKRIEKELKEIEEKERKLR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 301 RENCTLDTECHEKEKHINQLQTkvavLEQEIKDKDQLvlrtkEAFDtIQEQKVALEENgEKNQIQLGKLEATIKSLSAEL 380
Cdd:PRK03918 480 KELRELEKVLKKESELIKLKEL----AEQLKELEEKL-----KKYN-LEELEKKAEEY-EKLKEKLIKLKGEIKSLKKEL 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 381 LKANEIIKKL----------QGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQL 450
Cdd:PRK03918 549 EKLEELKKKLaelekkldelEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEEL 628
|
330 340 350
....*....|....*....|....*....|....*...
gi 564338581 451 ETTVQKLEESKQLLKNNEKLITWLNKELNENQLGRKQD 488
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE 666
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
250-470 |
2.31e-08 |
|
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: 56.83 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 250 LQNRLSELEAANKELterkykgdstVRELKAKLAGVEEELQRTKqevlslrRENCTLDTECHEKEKHINQLQTKVAVLEQ 329
Cdd:pfam07888 32 LQNRLEECLQERAEL----------LQAQEAANRQREKEKERYK-------RDREQWERQRRELESRVAELKEELRQSRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 330 EIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTI 409
Cdd:pfam07888 95 KHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERK 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564338581 410 QQEKLLAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKL 470
Cdd:pfam07888 175 QLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
163-440 |
2.50e-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: 57.39 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 163 EKLSLTKSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTAALT--NKHSQELTNEKEKALQTQVQYQQQHEQQKKDLE 240
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEelNKKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 241 ALHQRNIHQLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHE-KEKH--- 316
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtRDELkdy 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 317 ----------INQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEI 386
Cdd:TIGR02169 391 rekleklkreINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 564338581 387 IKKLQGDLKTLMGKLKlkntvtiQQEKLLAEKEemlqKERKESQDAGQSLRAKE 440
Cdd:TIGR02169 471 LYDLKEEYDRVEKELS-------KLQRELAEAE----AQARASEERVRGGRAVE 513
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
249-462 |
4.69e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 4.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 249 QLQNRLSELEAANKELTERkykgdstVRELKAKLAGVEEELQRTKQE--VLSLRRENCTLDTEchekekhINQLQTKVAV 326
Cdd:COG3206 165 NLELRREEARKALEFLEEQ-------LPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQ-------LSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 327 LEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQI--QLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK-- 402
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLraQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQqe 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564338581 403 -------LKNTVTI--QQEKLLAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQ 462
Cdd:COG3206 311 aqrilasLEAELEAlqAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARL 379
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
277-478 |
1.02e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.46 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 277 ELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDK-------DQLVLRTKEAFDTIQ 349
Cdd:TIGR02169 685 GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELeedlsslEQEIENVKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 350 EQKVALEENGEKNQIQLGKLEAT-----IKSLSAELLKANEIIKKLQGDLKTLMGKLKlkntvtiqqeKLLAEKeEMLQK 424
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARlshsrIPEIQAELSKLEEEVSRIEARLREIEQKLN----------RLTLEK-EYLEK 833
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 564338581 425 ERKESQDAGQSLRAKEQEVCRLQEQLETtvqKLEESKQLLKNNEKLITWLNKEL 478
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIENLNG---KKEELEEELEELEAALRDLESRL 884
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
237-443 |
2.02e-07 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.23 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 237 KDLEALHQrnIHQLQNRLSELEAANKELTERkykgdstVRELKAKLAGVEEELQRTKQEVLSLRREnctldtechekekh 316
Cdd:COG1579 4 EDLRALLD--LQELDSELDRLEHRLKELPAE-------LAELEDELAALEARLEAAKTELEDLEKE-------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 317 inqlqtkVAVLEQEIKDKDQLVLRTKEAFDTIQEQK--VALeengeknQIQLGKLEATIKSLSAELLKANEIIKKLQGDL 394
Cdd:COG1579 61 -------IKRLELEIEEVEARIKKYEEQLGNVRNNKeyEAL-------QKEIESLKRRISDLEDEILELMERIEELEEEL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 564338581 395 KTLMGKLKlkntvtiQQEKLLAEKEEMLQKERKESQDAGQSLRAKEQEV 443
Cdd:COG1579 127 AELEAELA-------ELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
249-480 |
2.26e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 249 QLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQR---TKQEVLSLRRENCTLDTECHEKEKHINQLQTKVA 325
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEleeLKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 326 VLEQEIKDKDQLVLRTKE------AFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEI---IKKLQGDLKT 396
Cdd:PRK03918 270 ELKKEIEELEEKVKELKElkekaeEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerLEELKKKLKE 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 397 LMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLitwLNK 476
Cdd:PRK03918 350 LEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE---LKK 426
|
....
gi 564338581 477 ELNE 480
Cdd:PRK03918 427 AIEE 430
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
287-474 |
1.23e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 287 EELQRTKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLvlrtKEAFDTIQEQKvALEENGEKNQIQL 366
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKL----LQLLPLYQELE-ALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 367 GKLEA---TIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQeklLAEKEEMLQKERKESQDAgqsLRAKEQEV 443
Cdd:COG4717 149 EELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLAELEEE---LEEAQEEL 222
|
170 180 190
....*....|....*....|....*....|.
gi 564338581 444 CRLQEQLETTVQKLEESKQLLKNNEKLITWL 474
Cdd:COG4717 223 EELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
286-486 |
2.13e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.22 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 286 EEELQRTKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDkdqlvlrtkeafdtIQEQKVALEENGEKNQIQ 365
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE--------------IEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 366 LGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgklklkntvtiqQEKLLAEKEEMLQKERKES----QDAGQSLRAKEQ 441
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEEL-------------EEDLHKLEEALNDLEARLShsriPEIQAELSKLEE 805
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 564338581 442 EVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQLGRK 486
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIK 850
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
260-419 |
2.40e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 260 ANKELTERKYKGDSTVRELKAKL-AGVEEELQRTKQEVLSLRREnctLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLV 338
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKEAeAIKKEALLEAKEEIHKLRNE---FEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 339 LRTKEAFDTIQEQKVALEEngeknqiQLGKLEATIKSLSAELLKANEIIKKLQGD------LKTLMGKLKLKNTVTIQQE 412
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQ-------ELEKKEEELEELIEEQLQELERISGLTAEeakeilLEKVEEEARHEAAVLIKEI 178
|
....*..
gi 564338581 413 KLLAEKE 419
Cdd:PRK12704 179 EEEAKEE 185
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
160-471 |
2.51e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 2.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 160 SKEEKLSLTKSLDDVTRQLHITQETLSEKMQELDKLRSEwashtaaLTNKHSQELTNEKEKAlqtqvqyqqqheQQKKDL 239
Cdd:PRK03918 201 ELEEVLREINEISSELPELREELEKLEKEVKELEELKEE-------IEELEKELESLEGSKR------------KLEEKI 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 240 EALHQRnIHQLQNRLSELEAANKELTERKYKGDSTVR------ELKAKLAGVEEELQRTKQEVLSLRRENctldTECHEK 313
Cdd:PRK03918 262 RELEER-IEELKKEIEELEEKVKELKELKEKAEEYIKlsefyeEYLDELREIEKRLSRLEEEINGIEERI----KELEEK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 314 EKHINQLQTKvavlEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQI-QLGKLEATIKSLSAELLKANEIIKKLQG 392
Cdd:PRK03918 337 EERLEELKKK----LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564338581 393 DLKTLMGKLKLKNTVTIQQEKllAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLI 471
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKK--AKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL 489
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
190-398 |
3.04e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 190 QELDKLRSEWASHTAALTNKHSQELTNEKEKALQTQVQYQQQHEqqkKDLEALHQRnIHQLQNRLSELEAANKELterky 269
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE---IDVASAERE-IAELEAELERLDASSDDL----- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 270 kgdstvRELKAKLAGVEEELQRTKQEvlslrrenctldtechekekhINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQ 349
Cdd:COG4913 688 ------AALEEQLEELEAELEELEEE---------------------LDELKGEIGRLEKELEQAEEELDELQDRLEAAE 740
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 564338581 350 E-QKVALEENGEK--NQIQLGKLEATI-KSLSAELLKANEIIKKLQGDLKTLM 398
Cdd:COG4913 741 DlARLELRALLEErfAAALGDAVERELrENLEERIDALRARLNRAEEELERAM 793
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
212-476 |
3.25e-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: 50.56 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 212 QELTNEKEKALQTQVQYQQQHEQQKKDLEALHQRNIHQlQNRLSELEAANKELTerkykgdSTVRELKAKLAGVEEELQR 291
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEE-KNALQEQLQAETELC-------AEAEEMRARLAARKQELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 292 TKQEvlslrrenctLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEA 371
Cdd:pfam01576 76 ILHE----------LESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLED 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 372 TIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLE 451
Cdd:pfam01576 146 QNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIA 225
|
250 260
....*....|....*....|....*.
gi 564338581 452 TTVQKLEESK-QLLKNNEKLITWLNK 476
Cdd:pfam01576 226 ELQAQIAELRaQLAKKEEELQAALAR 251
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
243-480 |
3.69e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.04 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 243 HQRNIHQLQNRLSELEAANKEL---TERKYKGDSTVRELKAKLAGVEEELQRTKQEV-LSLRRENCTLDT---ECHEKEK 315
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLlaeAGLDDADAEAVEARREELEDRDEELRDRLEECrVAAQAHNEEAESlreDADDLEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 316 HINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLK 395
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 396 TLMGKLKLKNTV--------------------TI-----QQEKLLAEKEEM--LQKERKESQDAGQSLRAKEQEVCRLQE 448
Cdd:PRK02224 437 TARERVEEAEALleagkcpecgqpvegsphveTIeedreRVEELEAELEDLeeEVEEVEERLERAEDLVEAEDRIERLEE 516
|
250 260 270
....*....|....*....|....*....|..
gi 564338581 449 QLETTVQKLEESKQLLKNNEKLITWLNKELNE 480
Cdd:PRK02224 517 RREDLEELIAERRETIEEKRERAEELRERAAE 548
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
249-482 |
4.03e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 249 QLQNRLSELEAANKELterkykgdstvRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLE 328
Cdd:COG4372 32 QLRKALFELDKLQEEL-----------EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 329 QEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVT 408
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564338581 409 IQQEKLLAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQ 482
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
317-482 |
4.08e-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: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 317 INQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKT 396
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 397 LMGKLKlKNTVTIQQ------EKLLAEKEEMLQKER---------KESQDAGQSLRAKEQEVCRLQEQLETTVQKLEesk 461
Cdd:COG4942 102 QKEELA-ELLRALYRlgrqppLALLLSPEDFLDAVRrlqylkylaPARREQAEELRADLAELAALRAELEAERAELE--- 177
|
170 180
....*....|....*....|.
gi 564338581 462 QLLKNNEKLITWLNKELNENQ 482
Cdd:COG4942 178 ALLAELEEERAALEALKAERQ 198
|
|
| HD_XRCC4-like_N |
cd22210 |
N-terminal head domain found in the XRCC4 superfamily of proteins; The XRCC4 superfamily ... |
41-144 |
6.85e-06 |
|
N-terminal head domain found in the XRCC4 superfamily of proteins; The XRCC4 superfamily includes five families: XRCC4, XLF, PAXX, SAS6 and CCDC61. XRCC4 (X-ray repair cross-complementing protein 4), XLF (XRCC4-like factor) and PAXX (paralog of XRCC4 and XLF) play crucial roles in the non-homologous end-joining (NHEJ) DNA repair pathway. SAS6 (spindle assembly abnormal protein 6) and CCDC61 (coiled-coil domain-containing protein 61) have a centrosomal/centriolar function. Members of this superfamily have an N-terminal globular head domain, a centrally located coiled-coil, and a C-terminal low-complexity region. They form homodimers through two homodimerization domains: an N-terminal globular head domain and a parallel coiled-coil domain. In addition, some members such as XRCC4 and XLF form symmetric heterodimers that interact through their globular head domains at the opposite end of the homodimer interface, and may form XLF-XRCC4 filaments. This model corresponds to the N-terminal head domain of XRCC4 superfamily proteins.
Pssm-ID: 408999 Cd Length: 115 Bit Score: 45.61 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 41 RKDLVIRLTDDtdpFFLYNLVISEEDFQSLKLQQGLLVDFLSFPQKFIDLLQQCmqehVKETPRFLLQLTSSAALLdnsp 120
Cdd:cd22210 25 ERGLRLHVSDD---AFLWTGEVSESDISQLKNDQGILVDFASFPGKLRSALEKC----ILASDRFTFVLTIRGDEA---- 93
|
90 100
....*....|....*....|....
gi 564338581 121 vFLNVVETNPFKhLIHLSLKLLPG 144
Cdd:cd22210 94 -YLKLVEILDEQ-LPHITFALRKV 115
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
211-482 |
8.82e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.20 E-value: 8.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 211 SQELTNEKEKALQTQVQYQQQHEQQKKDLEALHQRNIHQLQNRLSELEAANKELTERKYKGDSTVRELKaklagVEEELQ 290
Cdd:pfam02463 165 SRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK-----LNEERI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 291 RTKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLE-QEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKL 369
Cdd:pfam02463 240 DLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEeKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 370 EATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQ----QEKLLAEKEEMLQKERKESQDAGQSLRAKEQEVCR 445
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEEleklQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
250 260 270
....*....|....*....|....*....|....*..
gi 564338581 446 LQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQ 482
Cdd:pfam02463 400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEE 436
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
217-385 |
9.53e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 9.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 217 EKEKALQTQVQYQQQHEQQKKDLEALHQRnIHQLQNRLSELEAANKELT--ERKYKGDSTVRELKAKLAGVEEELQRTKQ 294
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEE-LEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 295 EVLSLRRenctLDTECHEKEKHINQLQTKVAVLEQEIK-DKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATI 373
Cdd:COG4717 154 RLEELRE----LEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170
....*....|..
gi 564338581 374 KSLSAELLKANE 385
Cdd:COG4717 230 EQLENELEAAAL 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
252-470 |
1.38e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 252 NRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVlslrrenctldtecHEKEKHINQLQTKVAVLEQEI 331
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREI--------------NEISSELPELREELEKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 332 KDKDQlvlrTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIK---KLQGDLKTL--MGKLKLKNT 406
Cdd:PRK03918 231 KELEE----LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKelkELKEKAEEYikLSEFYEEYL 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564338581 407 VTIQQ-EKLLAEKEEMLQ------KERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKL 470
Cdd:PRK03918 307 DELREiEKRLSRLEEEINgieeriKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERL 377
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
246-479 |
1.78e-05 |
|
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: 47.71 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 246 NIHQLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKEKHI-------N 318
Cdd:TIGR04523 118 QKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIdkiknklL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 319 QLQTKVAVLEQEIKDKDQLVLRTKEafdtIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKaneiIKKLQGDLKTlm 398
Cdd:TIGR04523 198 KLELLLSNLKKKIQKNKSLESQISE----LKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ----LKDEQNKIKK-- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 399 gKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQSlraKEQEVCR-LQEQLETTVQKLEESKQLLKNNEKLITWLNKE 477
Cdd:TIGR04523 268 -QLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ---KEQDWNKeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQ 343
|
..
gi 564338581 478 LN 479
Cdd:TIGR04523 344 IS 345
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
182-433 |
2.88e-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: 46.68 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 182 QETLSEKMQELDKLRSEwashtAALTNKHSQELTNEKEKALqtqvqyqqqheqqkKDLEALhQRNIHQLQNRLSELEAAN 261
Cdd:COG4942 19 ADAAAEAEAELEQLQQE-----IAELEKELAALKKEEKALL--------------KQLAAL-ERRIAALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 262 KELTERkykgdstVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKE----KHINQLQTKVAVLEQEIKDKDQL 337
Cdd:COG4942 79 AALEAE-------LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 338 VLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAE 417
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250
....*....|....*.
gi 564338581 418 KEEMLQKERKESQDAG 433
Cdd:COG4942 232 LEAEAAAAAERTPAAG 247
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
148-478 |
3.42e-05 |
|
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: 46.94 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 148 EIKKFLAGCLKCSKEEKLSLTKSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTAALTNKHSQELTNEKEKAlqtqvq 227
Cdd:TIGR04523 307 DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ------ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 228 yqqqheqQKKDlealhqrNIHQLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLD 307
Cdd:TIGR04523 381 -------SYKQ-------EIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 308 TECHEKEKHINQLQTKVAVLEQEIKD---------------KDQLVLRTKEaFDTIQEQKVALEENGEKNQIQLGKLEAT 372
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVlsrsinkikqnleqkQKELKSKEKE-LKKLNEEKKELEEKVKDLTKKISSLKEK 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 373 IKSLSAELLKANEIIKKLQGDLKTL---MGKLKLKNTVTIQQEKLL-------------AEKEEMLQKERKESQDAGQSL 436
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDELNKDdfeLKKENLEKEIDEKNKEIEelkqtqkslkkkqEEKQELIDQKEKEKKDLIKEI 605
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 564338581 437 RAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKEL 478
Cdd:TIGR04523 606 EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEV 647
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
183-482 |
3.61e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 183 ETL-SEKMQELDKLRSEWASHTAALTNKHSQELTNEKEKALQTQVQYQQQHEQQK------KDLEALHQRNIHQLQNRLS 255
Cdd:pfam15921 248 EALkSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEiiqeqaRNQNSMYMRQLSDLESTVS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 256 ELEAankELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDtechekekhiNQLQTKVAVLEQeikdkd 335
Cdd:pfam15921 328 QLRS---ELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLD----------DQLQKLLADLHK------ 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 336 qlvlRTKEaFDTIQEQKVALEENGEKNQIqlgkleaTIKSLSAELLKANEIIKKLQGDLKTlmgklkLKNTVTIQQEKLL 415
Cdd:pfam15921 389 ----REKE-LSLEKEQNKRLWDRDTGNSI-------TIDHLRRELDDRNMEVQRLEALLKA------MKSECQGQMERQM 450
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564338581 416 AEKEemlqkERKESQDAGQSLRAKEQEVcrlQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQ 482
Cdd:pfam15921 451 AAIQ-----GKNESLEKVSSLTAQLEST---KEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE 509
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
157-480 |
3.77e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 157 LKCSKEEKLSLTKSLDDVTR---QLHITQETLSEKMQELDKLRSEWASHTAALTNKHSQ--ELTNEKEKALQTQVQYQQQ 231
Cdd:pfam01576 14 LQKVKERQQKAESELKELEKkhqQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQEleEILHELESRLEEEEERSQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 232 HEQQKKDLealhQRNIHQLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEE---LQRTKQEVLSLRRENCTLDT 308
Cdd:pfam01576 94 LQNEKKKM----QQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQnskLSKERKLLEERISEFTSNLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 309 ECHEKEKHINQLQTKVAVLEQEIKDkdqlvlRTKEAFDTIQEQ---KVALEENGEKNQIQLGKLEATIKSLSAELLKANE 385
Cdd:pfam01576 170 EEEEKAKSLSKLKNKHEAMISDLEE------RLKKEEKGRQELekaKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 386 IIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLLK 465
Cdd:pfam01576 244 ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRS 323
|
330
....*....|....*
gi 564338581 466 NNEKLITWLNKELNE 480
Cdd:pfam01576 324 KREQEVTELKKALEE 338
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
162-469 |
4.18e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.71 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 162 EEKLSLTKSLDDVTRQLHITQETLSEKMQELDKLR----SEWASHTAALTN---KHSQELtNEKEKALQTQVQYQQQHEQ 234
Cdd:pfam01576 299 EELEALKTELEDTLDTTAAQQELRSKREQEVTELKkaleEETRSHEAQLQEmrqKHTQAL-EELTEQLEQAKRNKANLEK 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 235 QKKDLEALHQrnihQLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKE 314
Cdd:pfam01576 378 AKQALESENA----ELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 315 KHINQLQTKVAVLEQEIKDKDQLV---LRTKEAFDT----IQEQKVALEENGEKNQIQLGKLEATIKSLSAELLkanEII 387
Cdd:pfam01576 454 GKNIKLSKDVSSLESQLQDTQELLqeeTRQKLNLSTrlrqLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLS---DMK 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 388 KKLQGDLKTLMGklklkntvtiqqekllaeKEEMLQKERKESQDAGQSLRAKEQEV-------CRLQEQLETTVQKLEES 460
Cdd:pfam01576 531 KKLEEDAGTLEA------------------LEEGKKRLQRELEALTQQLEEKAAAYdklektkNRLQQELDDLLVDLDHQ 592
|
....*....
gi 564338581 461 KQLLKNNEK 469
Cdd:pfam01576 593 RQLVSNLEK 601
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
152-384 |
8.23e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 152 FLAGCLKCSKEEKLSLTKSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTAALtnKHSQELTNEKEKALQTQVQYQQQ 231
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI--AALARRIRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 232 HEQQKKDLEALHQRNIHQLQNRLSELEAANK----------ELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRR 301
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLGRqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 302 EnctLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELL 381
Cdd:COG4942 168 E---LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
...
gi 564338581 382 KAN 384
Cdd:COG4942 245 AAG 247
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
204-462 |
8.83e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 204 AALTNKHSQELTNEKEKALQTQVQYQQQHEQQKKDLealhQRNIHQLQNRLSELEAANKELTERkykgdstVRELKAKLA 283
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARR-------IRALEQELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 284 GVEEELQRTKQEVLSLRREnctLDTECHEKEKHINQLQTkvavleQEIKDKDQLVLRTKEAFDTIQEQKV------ALEE 357
Cdd:COG4942 80 ALEAELAELEKEIAELRAE---LEAQKEELAELLRALYR------LGRQPPLALLLSPEDFLDAVRRLQYlkylapARRE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 358 NGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgklklkntvtiqqEKLLAEKEEMLQKERKESQDAGQSLR 437
Cdd:COG4942 151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAAL--------------EALKAERQKLLARLEKELAELAAELA 216
|
250 260
....*....|....*....|....*
gi 564338581 438 AKEQEVCRLQEQLETTVQKLEESKQ 462
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
157-487 |
1.08e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 157 LKCSKEEKLSLTKSLDDVTRQLHITQETLSEKMQELDKLRSEWAS-----------HTAALTNKHSQELTN--------- 216
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelteeHRKELLEEYTAELKRiekelkeie 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 217 EKEKALQTQVQYQQQHEQQKKDLEALHQRnIHQLQNRLSELEAANKELTERKYKGDSTVRE----LKAKLAGVEEELQRT 292
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESELIKLKEL-AEQLKELEEKLKKYNLEELEKKAEEYEKLKEklikLKGEIKSLKKELEKL 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 293 KQevlsLRRENCTLDTECHEKEKHINQLQTKVAVLEQE-IKDKDQLVLRTKEAFDTIQEQKVALEEngeknqiqLGKLEA 371
Cdd:PRK03918 552 EE----LKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELEPFYNEYLELKDAEKE--------LEREEK 619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 372 TIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNtVTIQQEKLLAEKEEMLQKERKESqdagqSLRAKEQEVCRLQEQLE 451
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELE-KKYSEEEYEELREEYLELSRELA-----GLRAELEELEKRREEIK 693
|
330 340 350
....*....|....*....|....*....|....*.
gi 564338581 452 TTVQKLEESKQLLKNNEKLITWLNKELNENQLGRKQ 487
Cdd:PRK03918 694 KTLEKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
246-461 |
1.11e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 246 NIHQLQNRLSELEAANKEL--TERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRREnctldtechEKEKHINQLQTK 323
Cdd:COG4913 226 AADALVEHFDDLERAHEALedAREQIELLEPIRELAERYAAARERLAELEYLRAALRLW---------FAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 324 VAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQ-IQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLmgKLK 402
Cdd:COG4913 297 LEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAAL--GLP 374
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564338581 403 LKNTVTI---QQEKLLAEKEEmLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESK 461
Cdd:COG4913 375 LPASAEEfaaLRAEAAALLEA-LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
183-494 |
1.14e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 183 ETLSEKMQELDKLRSEWASHTAALtnkhsQELTNEKEKALQTQVQYQQQHEQQKKDLEALHQRN-IHQLQNRLSELEAAN 261
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEEL-----EELEEELEELEAELEELREELEKLEKLLQLLPLYQeLEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 262 KELTERKykgdSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTldtechEKEKHINQLQTKVAVLEQEIKDKDQLVLRT 341
Cdd:COG4717 149 EELEERL----EELRELEEELEELEAELAELQEELEELLEQLSL------ATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 342 KEAFDTIQEQKVALEENGEKNQI--QLGKLEATIKSLSAeLLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKE 419
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALeeRLKEARLLLLIAAA-LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 420 EMLQKERKESQDAGQSLRAKEQEVCRL-----------QEQLETTVQKLEESKQLLKNNEKlitwLNKELNENQLGRKQD 488
Cdd:COG4717 298 ASLGKEAEELQALPALEELEEEELEELlaalglppdlsPEELLELLDRIEELQELLREAEE----LEEELQLEELEQEIA 373
|
....*.
gi 564338581 489 TLGASA 494
Cdd:COG4717 374 ALLAEA 379
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
183-480 |
1.16e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 183 ETLSEKMQEldKLRSEWASHTAALTNKhSQELTNEKEKAlQTQVQYQQQHEQQKKDLEALHQRNIHQLQNRLSELEAANK 262
Cdd:PTZ00121 1460 EEAKKKAEE--AKKADEAKKKAEEAKK-ADEAKKKAEEA-KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK 1535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 263 ELTERKYKGDSTVREL-KAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRT 341
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELkKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA 1615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 342 KEAfdTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEM 421
Cdd:PTZ00121 1616 EEA--KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA 1693
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564338581 422 LQKERKESQDAGQsLRAKEQEVCRLQEQL----ETTVQKLEESKQLLKNNEKLITWLNKELNE 480
Cdd:PTZ00121 1694 LKKEAEEAKKAEE-LKKKEAEEKKKAEELkkaeEENKIKAEEAKKEAEEDKKKAEEAKKDEEE 1755
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
183-477 |
1.45e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 183 ETLSEKMQELDKLRSEwaSHTAALTNKHSQEL--TNEKEKALQTQVQYQQQHEQQKKDLEALHQRNIHQLQNRLSELEAA 260
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADE--AKKAAEAKKKADEAkkAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEK 1563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 261 NKELTERKYKGDSTVRELKAKLAGVEEElqRTKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLR 340
Cdd:PTZ00121 1564 KKAEEAKKAEEDKNMALRKAEEAKKAEE--ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 341 TKEAFDTIQEQKVALEENGEKNQiQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLaEKEE 420
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAA-EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEK-KKAE 1719
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 564338581 421 MLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKE 477
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
348-459 |
1.53e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 348 IQEQKVALEENGEKNQIQLGKLEAtiKSLSAE-LLKANEIIKKLQ----GDLKTLMGKLKLKNTVTIQQEKLLAEKEEML 422
Cdd:PRK12704 28 IAEAKIKEAEEEAKRILEEAKKEA--EAIKKEaLLEAKEEIHKLRnefeKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110
....*....|....*....|....*....|....*..
gi 564338581 423 QKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEE 459
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
161-356 |
1.57e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 161 KEEKLSLTKSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTAALTNKHSQ---------ELTNEKEKALQTQVQYQQQ 231
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAElaeaeeeleELAEELLEALRAAAELAAQ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 232 HEQQKKDLEALHQRnIHQLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECH 311
Cdd:COG1196 402 LEELEEAEEALLER-LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 564338581 312 EKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALE 356
Cdd:COG1196 481 ELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
144-468 |
2.19e-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: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 144 GN-DVEIKKFLAGCLKcsKEEKLSLTK---------------SLDDVTRQLHITQETLSEKMQELDKLRSE----WASHT 203
Cdd:pfam15921 373 GNlDDQLQKLLADLHK--REKELSLEKeqnkrlwdrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSEcqgqMERQM 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 204 AALTNKHSQ-----ELTNEKEKALQTQVQYQQQHEQQKKDLEAlHQRNIHQLQNRLSE----LEAANKELTERKYKGDST 274
Cdd:pfam15921 451 AAIQGKNESlekvsSLTAQLESTKEMLRKVVEELTAKKMTLES-SERTVSDLTASLQEkeraIEATNAEITKLRSRVDLK 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 275 VRELKaKLAGVEEELQRTKQEVLSLRrenctldTECHEKEKHINqlqtkvaVLEQEIKDKDQLVLRTKEAFDTIQEQKVA 354
Cdd:pfam15921 530 LQELQ-HLKNEGDHLRNVQTECEALK-------LQMAEKDKVIE-------ILRQQIENMTQLVGQHGRTAGAMQVEKAQ 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 355 LEEN--------------GEKNQIQLGKLEATIKSLSAELLK-ANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKL--LAE 417
Cdd:pfam15921 595 LEKEindrrlelqefkilKDKKDAKIRELEARVSDLELEKVKlVNAGSERLRAVKDIKQERDQLLNEVKTSRNELnsLSE 674
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 564338581 418 KEEMLQKE-RKESQDAgqslrakEQEVCRLQEQLETTVQKLEESKQLLKNNE 468
Cdd:pfam15921 675 DYEVLKRNfRNKSEEM-------ETTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
148-482 |
2.30e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 44.57 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 148 EIKKFLAGCLKCSKEEKLSLTKSLDDVTRQLHITQETLSEKMQEL-DKLRSEWASHTAALTNKHSQELTNEKEKALQTQv 226
Cdd:TIGR00618 187 AKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLrEALQQTQQSHAYLTQKREAQEEQLKKQQLLKQL- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 227 qyqqqheqqkkdlealhQRNIHQLQNRLSELEAANKELTERKYKG-----DSTVRELKAKLAGVEEELQRTKQEVLSLRR 301
Cdd:TIGR00618 266 -----------------RARIEELRAQEAVLEETQERINRARKAAplaahIKAVTQIEQQAQRIHTELQSKMRSRAKLLM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 302 ENCTLDTECHEKEKHINQLQTkvaVLEQEIKDKDQLVLRTkeAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELl 381
Cdd:TIGR00618 329 KRAAHVKQQSSIEEQRRLLQT---LHSQEIHIRDAHEVAT--SIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEL- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 382 kanEIIKKLQGDLKTLMGKLKlkntvTIQQEKLLAEKEEMLQKERKE-----SQDAGQSLRAKEQEVCRLQEQLETTVQK 456
Cdd:TIGR00618 403 ---DILQREQATIDTRTSAFR-----DLQGQLAHAKKQQELQQRYAElcaaaITCTAQCEKLEKIHLQESAQSLKEREQQ 474
|
330 340
....*....|....*....|....*.
gi 564338581 457 LEESKQLLKNNEKLITWLNKELNENQ 482
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQ 500
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
166-366 |
2.91e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 166 SLTKSLDDVTRQLHITQETLSEKMQELDKLRSE----WASHTAALTNKHSQELTNEKEKALQTQVQYQQQHEQQKKDL-- 239
Cdd:COG3206 172 EARKALEFLEEQLPELRKELEEAEAALEEFRQKnglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLgs 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 240 ------EALHQRNIHQLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVL-SLRRENCTLDTECHE 312
Cdd:COG3206 252 gpdalpELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILaSLEAELEALQAREAS 331
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 564338581 313 KEKHINQLQTKVAVL---EQEIKDKDQLVLRTKEAFDTIQE--QKVALEENGEKNQIQL 366
Cdd:COG3206 332 LQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQrlEEARLAEALTVGNVRV 390
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
272-470 |
2.94e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 272 DSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQ 351
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 352 KVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLK-LKNTVTIQQEKLLAEKEEMLQKERKESQ 430
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLEsLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 564338581 431 DAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKL 470
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA 229
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
236-485 |
3.57e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 43.76 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 236 KKDLEALHQRNIHQLQNRLSEL-----EAANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLslrrenctldtec 310
Cdd:PRK05771 37 KEELSNERLRKLRSLLTKLSEAldklrSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIK------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 311 hEKEKHINQLQTKVAVLEQEIKDKDQLvlrtkEAFDTiqeqKVALEENGEKNQIQLGKLEATIKS-LSAELLKANEIIKK 389
Cdd:PRK05771 104 -ELEEEISELENEIKELEQEIERLEPW-----GNFDL----DLSLLLGFKYVSVFVGTVPEDKLEeLKLESDVENVEYIS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 390 lqgdlktlmgKLKLKNTVTIQQEKLLAEK-EEMLQK---ERKESQDAG---QSLRAKEQEVCRLQEQLETTVQKLEESKQ 462
Cdd:PRK05771 174 ----------TDKGYVYVVVVVLKELSDEvEEELKKlgfERLELEEEGtpsELIREIKEELEEIEKERESLLEELKELAK 243
|
250 260
....*....|....*....|...
gi 564338581 463 llKNNEKLITWlnKELNENQLGR 485
Cdd:PRK05771 244 --KYLEELLAL--YEYLEIELER 262
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
238-333 |
3.92e-04 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 41.88 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 238 DLEAlHQRNIHQLQNRLSEL----EAANKELTERKyKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEK 313
Cdd:pfam05266 79 ELEK-HGFDVKAPQSRINKLlslkDRQTKLLEELK-KLEKKIAEEESEKRKLEEEIDELEKKILELERQLALAKEKKEAA 156
|
90 100
....*....|....*....|
gi 564338581 314 EKHINQLQTKVAVLEQEIKD 333
Cdd:pfam05266 157 DKEIARLKSEAEKLEQEIQD 176
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
160-451 |
4.60e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 160 SKEEKLSLTKSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTAAL--TNKHSQELTNEKEKALQTQVQYQQQHEQQKK 237
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELeqLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 238 DLEALHQRnIHQLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKE--K 315
Cdd:COG4372 109 EAEELQEE-LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAldE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 316 HINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLK 395
Cdd:COG4372 188 LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAI 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 564338581 396 TLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLE 451
Cdd:COG4372 268 LVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
247-465 |
5.63e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.90 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 247 IHQLQN----RLSELEAANKELTERKY-----KGDSTVRELKAKLAGVEEELQRTKQEVLSlrrenctldtechEKEKHI 317
Cdd:PRK04778 221 LKELQTelpdQLQELKAGYRELVEEGYhldhlDIEKEIQDLKEQIDENLALLEELDLDEAE-------------EKNEEI 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 318 N-QLQTKVAVLEQEIKDK---DQLVLRTKEAFDTIQEQKVALEEN----GEKNQIQLGKLEaTIKSLSAELlkaNEIIKK 389
Cdd:PRK04778 288 QeRIDQLYDILEREVKARkyvEKNSDTLPDFLEHAKEQNKELKEEidrvKQSYTLNESELE-SVRQLEKQL---ESLEKQ 363
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564338581 390 LQGDLKTLMGKLKLKNTVTIQQEKLLaEKEEMLQKERKESQDAGQSLRAKEQEVcrlQEQLETTVQKLEESKQLLK 465
Cdd:PRK04778 364 YDEITERIAEQEIAYSELQEELEEIL-KQLEEIEKEQEKLSEMLQGLRKDELEA---REKLERYRNKLHEIKRYLE 435
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
239-464 |
7.29e-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: 42.50 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 239 LEALHQRNIHQLQNRLSELEAANKELterkykgdstvRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKEKHIN 318
Cdd:pfam10174 452 IERLKEQREREDRERLEELESLKKEN-----------KDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLK 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 319 QLqtkvavlEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQiqlgkleaTIKSLSAELLKANEIIKKLQGDLKTLM 398
Cdd:pfam10174 521 SL-------EIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEIND--------RIRLLEQEVARYKEESGKAQAEVERLL 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 399 GKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQSLRAKEQEV--------------------CRLQEQLETTVQKLE 458
Cdd:pfam10174 586 GILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMkkkgaqlleearrrednladNSQQLQLEELMGALE 665
|
....*.
gi 564338581 459 ESKQLL 464
Cdd:pfam10174 666 KTRQEL 671
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
176-436 |
7.54e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 176 RQLHITQETLSEKMQELDKLRSEWASHTAALTNKHSQELTNEKEKALQTQVQYQQQHEQQKKDLE--ALHQRNIHQLQNR 253
Cdd:pfam12128 276 SRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIEtaAADQEQLPSWQSE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 254 LSELEAANKELT------ERKYKG--DSTVRELKAKLAGVEEELQRTKQE-VLSLRRENCTLDTECHEKEKHINQLQTKV 324
Cdd:pfam12128 356 LENLEERLKALTgkhqdvTAKYNRrrSKIKEQNNRDIAGIKDKLAKIREArDRQLAVAEDDLQALESELREQLEAGKLEF 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 325 AVLEQEIKDK-DQLVLRTKEAfdTIQEQkvaLEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKL 403
Cdd:pfam12128 436 NEEEYRLKSRlGELKLRLNQA--TATPE---LLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQ 510
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 564338581 404 KNTVTIQQEKLLAEKEEMLQKE--------RKESQDAGQSL 436
Cdd:pfam12128 511 ASRRLEERQSALDELELQLFPQagtllhflRKEAPDWEQSI 551
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
253-456 |
1.17e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 253 RLSELEAANKELTERkykgdstVRELKAKLAGVEEELQRTKQevlslRRENCTLDTECHEKEKHINQLQTKVAVLEQEIK 332
Cdd:COG4913 611 KLAALEAELAELEEE-------LAEAEERLEALEAELDALQE-----RREALQRLAEYSWDEIDVASAEREIAELEAELE 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 333 DkdqlVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLmGKLKLKNTVTIQQE 412
Cdd:COG4913 679 R----LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA-EDLARLELRALLEE 753
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 564338581 413 KLLAEKEEmlQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQK 456
Cdd:COG4913 754 RFAAALGD--AVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
237-389 |
1.19e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 237 KDLEALHQRNIHQLQNRLSELEAANKELTERKykgdSTVRELKAKLAGVEEELQ--RTKQEVLSLRRENCTLDTECHEKE 314
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLE----LEIEEVEARIKKYEEQLGnvRNNKEYEALQKEIESLKRRISDLE 109
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564338581 315 KHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQL-GKLEATIKSLSAELLKANEIIKK 389
Cdd:COG1579 110 DEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELeAEREELAAKIPPELLALYERIRK 185
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
157-458 |
1.31e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 157 LKCSKEEKLSLTKSLDDVTRQLHITQETLSE-------KMQELDKLRSEWASHTAALTNKHSQEL-TNEKEKALQTQVQY 228
Cdd:pfam15921 491 LESSERTVSDLTASLQEKERAIEATNAEITKlrsrvdlKLQELQHLKNEGDHLRNVQTECEALKLqMAEKDKVIEILRQQ 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 229 QQQHEQqkkdLEALHQRNIHQLQNRLSELEaanKELTER----------KYKGDSTVRELKAKLAGVeeELQRTK----- 293
Cdd:pfam15921 571 IENMTQ----LVGQHGRTAGAMQVEKAQLE---KEINDRrlelqefkilKDKKDAKIRELEARVSDL--ELEKVKlvnag 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 294 ----QEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDK--------DQLVLRTKEAFDTIQEQKVALEEN--- 358
Cdd:pfam15921 642 serlRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKseemetttNKLKMQLKSAQSELEQTRNTLKSMegs 721
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 359 ---------GEKNQI-----QLGKLEATIKSLSAELLKAN-------EIIKKLQGDLKTLM---GKLKLKNTVTIQQEKL 414
Cdd:pfam15921 722 dghamkvamGMQKQItakrgQIDALQSKIQFLEEAMTNANkekhflkEEKNKLSQELSTVAtekNKMAGELEVLRSQERR 801
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 564338581 415 LAEK----EEMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLE 458
Cdd:pfam15921 802 LKEKvanmEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKELQ 849
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
183-475 |
1.35e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 183 ETLSEKMQELDKLRSEWAS---HTAALTNKHsqeltnEKEKALQTQVQYQQQHEQQKKDLEALhqrnIHQLQNRLSELEA 259
Cdd:PRK02224 468 ETIEEDRERVEELEAELEDleeEVEEVEERL------ERAEDLVEAEDRIERLEERREDLEEL----IAERRETIEEKRE 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 260 ANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTEchekekhINQLQTKVAVLEqEIKDKDQLVL 339
Cdd:PRK02224 538 RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKER-------IESLERIRTLLA-AIADAEDEIE 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 340 RTKEAFDTIQEQ----KVALEENGEKNQIQLGKL-EATIKSLSAELLKANEIIKKLQGDLKTLMGKL-KLKNTVTIQQEK 413
Cdd:PRK02224 610 RLREKREALAELnderRERLAEKRERKRELEAEFdEARIEEAREDKERAEEYLEQVEEKLDELREERdDLQAEIGAVENE 689
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564338581 414 LlaEKEEMLQKERKESQDAGQSLRAKEQEVcrlqEQLETTVQKLE-ESKQllKNNEKLITWLN 475
Cdd:PRK02224 690 L--EELEELRERREALENRVEALEALYDEA----EELESMYGDLRaELRQ--RNVETLERMLN 744
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
182-476 |
1.39e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 182 QETLSEKMQELDK----LRSEWASHTAALTnKHSQELTNEKEKAlQTQVQYQQQHEQQKKDLEALHQRNIHQLQNRLSEL 257
Cdd:PRK02224 309 AEAVEARREELEDrdeeLRDRLEECRVAAQ-AHNEEAESLREDA-DDLEERAEELREEAAELESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 258 EAANKELTE-RKYKGDSTVR--ELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKEkhinQLQT--KVAVLEQEIK 332
Cdd:PRK02224 387 EELEEEIEElRERFGDAPVDlgNAEDFLEELREERDELREREAELEATLRTARERVEEAE----ALLEagKCPECGQPVE 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 333 DKdqlvlrtkEAFDTIQEQKVALEENGEknqiQLGKLEATIKSLSAELLKANEIiKKLQGDLKTLMGKLKLKNTVTIQQE 412
Cdd:PRK02224 463 GS--------PHVETIEEDRERVEELEA----ELEDLEEEVEEVEERLERAEDL-VEAEDRIERLEERREDLEELIAERR 529
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564338581 413 KLLAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNK 476
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER 593
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
162-472 |
1.41e-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: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 162 EEKLSLTKSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTAALTNKHSQE---------LTNEKEKALQTQVQYQQQH 232
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLadareviscLKNELSELRRQIQRAELEL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 233 EQQKKDLEALHQR------NIHQLQNRLSELEAANKELTERKYKgdstVRELKAKLAGVE---EELQRTKQEVLSLRREN 303
Cdd:pfam05557 128 QSTNSELEELQERldllkaKASEAEQLRQNLEKQQSSLAEAEQR----IKELEFEIQSQEqdsEIVKNSKSELARIPELE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 304 CTLDtECHEKEKHINQLQTKVAVLEQEIKDkdqlvLRTK-EAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLK 382
Cdd:pfam05557 204 KELE-RLREHNKHLNENIENKLLLKEEVED-----LKRKlEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 383 ----ANEIIKKLQGDLkTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLE 458
Cdd:pfam05557 278 pedlSRRIEQLQQREI-VLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERD 356
|
330
....*....|....
gi 564338581 459 ESKQLLKNNEKLIT 472
Cdd:pfam05557 357 GYRAILESYDKELT 370
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
246-480 |
1.41e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 246 NIHQLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKEKHINQLQTkva 325
Cdd:TIGR04523 69 KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLT--- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 326 vleqEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKklqgDLKTLMGKLKLKN 405
Cdd:TIGR04523 146 ----EIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLS----NLKKKIQKNKSLE 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564338581 406 TVTIQQEKLLAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNE 480
Cdd:TIGR04523 218 SQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQ 292
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
283-469 |
1.50e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 283 AGVEEELQRTKQEVLSLRRENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKN 362
Cdd:pfam02463 162 AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 363 QIQLGKLE-ATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQDAGQSLRAKEQ 441
Cdd:pfam02463 242 LQELLRDEqEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEK 321
|
170 180
....*....|....*....|....*...
gi 564338581 442 EVCRLQEQLETTVQKLEESKQLLKNNEK 469
Cdd:pfam02463 322 EKKKAEKELKKEKEEIEELEKELKELEI 349
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
243-482 |
1.61e-03 |
|
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: 41.65 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 243 HQRNI--HQLQNRLSELEAAN-KELTERKYKGDSTVRELKAKLAGVEEELQR-----TKQEVLSLRRENCTLDTECHEKE 314
Cdd:pfam17380 280 HQKAVseRQQQEKFEKMEQERlRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaiyAEQERMAMERERELERIRQEERK 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 315 KHINQL-QTKVAVLEQEIKDKDQLVL-------RTKEAFDTIQEQKVALEENGEKNQIQLGKLEatikSLSAELLKANEI 386
Cdd:pfam17380 360 RELERIrQEEIAMEISRMRELERLQMerqqkneRVRQELEAARKVKILEEERQRKIQQQKVEME----QIRAEQEEARQR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 387 -IKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEMLQKERKESQdagqslraKEQEVCRLQEQLETTV--QKLEESKQL 463
Cdd:pfam17380 436 eVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELE--------KEKRDRKRAEEQRRKIleKELEERKQA 507
|
250
....*....|....*....
gi 564338581 464 LKNNEKLITWLNKELNENQ 482
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQ 526
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
249-470 |
1.62e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.05 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 249 QLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDT---ECHEKEKHINQL----Q 321
Cdd:COG1340 47 ELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKaggSIDKLRKEIERLewrqQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 322 TKVAVLEQEIkdkdQLVLRTKEAFDTIQEQKVALEENGEKNQI---------QLGKLEATIKSLSAELLKANEIIKKLQG 392
Cdd:COG1340 127 TEVLSPEEEK----ELVEKIKELEKELEKAKKALEKNEKLKELraelkelrkEAEEIHKKIKELAEEAQELHEEMIELYK 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 393 DLKTLMGKL-KLKNTVTIQQEKLLAEKEEM--LQKERKESQDAGQSLRAKEQEVcRLQEQLETTVQKLEESKQLLKNNEK 469
Cdd:COG1340 203 EADELRKEAdELHKEIVEAQEKADELHEEIieLQKELRELRKELKKLRKKQRAL-KREKEKEELEEKAEEIFEKLKKGEK 281
|
.
gi 564338581 470 L 470
Cdd:COG1340 282 L 282
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
153-459 |
1.71e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.42 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 153 LAGCLKCSKEEKLSLTKSLDDVTRQLHITQETLSEKMQELDKLRSEWASHTAALTN--KHSQELTNEKEKALQTQVQYQQ 230
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEelRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 231 QHEQQKKDL----EALHQR------NIHQLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLR 300
Cdd:pfam07888 112 ELSEEKDALlaqrAAHEARireleeDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 301 RENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLR---TKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLS 377
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAEneaLLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 378 AELLKANEIIKKLQGDLKTLMGKLK------------LKNTVTIQQEKL------LAEKEEMLQKERKESQDA------- 432
Cdd:pfam07888 272 AELHQARLQAAQLTLQLADASLALRegrarwaqeretLQQSAEADKDRIeklsaeLQRLEERLQEERMEREKLevelgre 351
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 564338581 433 --------------GQSLRAKEQEVCRLQEQLETTVQKLEE 459
Cdd:pfam07888 352 kdcnrvqlsesrreLQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
212-469 |
1.73e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.63 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 212 QELTNEKEKALQTQVQYQQQHEQQKKDLEALhqrnIHQLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELQR 291
Cdd:pfam05483 232 KKEINDKEKQVSLLLIQITEKENKMKDLTFL----LEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 292 TkqevLSLRRencTLDTECHEKEKHINQL-QTKVAVLEQEIKDKDQLVLRTKEAFDTIqeqkVALEENGEKNQIQLGKLE 370
Cdd:pfam05483 308 S----MSTQK---ALEEDLQIATKTICQLtEEKEAQMEELNKAKAAHSFVVTEFEATT----CSLEELLRTEQQRLEKNE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 371 ATIKSLSAELLKANEIIKKlqgdlktlMGKLKLKNTVTIQQ-EKLLAEKEEMLQkERKESQDAGQSLRAKEQEVCRLQEQ 449
Cdd:pfam05483 377 DQLKIITMELQKKSSELEE--------MTKFKNNKEVELEElKKILAEDEKLLD-EKKQFEKIAEELKGKEQELIFLLQA 447
|
250 260
....*....|....*....|
gi 564338581 450 LETTVQKLEESKQLLKNNEK 469
Cdd:pfam05483 448 REKEIHDLEIQLTAIKTSEE 467
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
236-480 |
1.75e-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: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 236 KKDLEALHQrNIHQLQNRLSELEAANKELTERKYKGDSTvRELKAKLAGVEEELQRTKQE--------------VLSLRR 301
Cdd:TIGR00606 597 NKELASLEQ-NKNHINNELESKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSKQramlagatavysqfITQLTD 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 302 EN---CTLDTECHEKEKHINQ----LQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIK 374
Cdd:TIGR00606 675 ENqscCPVCQRVFQTEAELQEfisdLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQ 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 375 SLSAELLKANEIIKKLQGDLKTLMGKLKLKN------TVTIQQEKLLAEKEEMLQKERKESQ--DAGQSLRAKEQEVCRL 446
Cdd:TIGR00606 755 KVNRDIQRLKNDIEEQETLLGTIMPEEESAKvcltdvTIMERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEKQEK 834
|
250 260 270
....*....|....*....|....*....|....
gi 564338581 447 QEQLETTVQKLEESKQLLKNNEKLITWLNKELNE 480
Cdd:TIGR00606 835 QHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE 868
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
157-479 |
1.83e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.25 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 157 LKCSKEEKLSLTKSLDDVTRQLH---ITQETLSEKMQ-------ELDKLRSEWASHTAALTNKHSQELTNEKEKALQTQV 226
Cdd:pfam05483 284 LKELIEKKDHLTKELEDIKMSLQrsmSTQKALEEDLQiatkticQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 227 QYQQQHEQQKKDLEALHQRNIhQLQNRLSELEaankELTERKYKGDSTVRELKAKLAGVEEELQRTKQ-----EVLSLRR 301
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITM-ELQKKSSELE----EMTKFKNNKEVELEELKKILAEDEKLLDEKKQfekiaEELKGKE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 302 ENCTLDTECHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKeaFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELL 381
Cdd:pfam05483 439 QELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTE--LEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELK 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 382 KANEII-------KKLQGDLKTLMGK-LKLKNTVTIQQEKLLAEKEEMLQKERKESQDA----------GQSLRAKEQEV 443
Cdd:pfam05483 517 KHQEDIinckkqeERMLKQIENLEEKeMNLRDELESVREEFIQKGDEVKCKLDKSEENArsieyevlkkEKQMKILENKC 596
|
330 340 350
....*....|....*....|....*....|....*.
gi 564338581 444 CRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELN 479
Cdd:pfam05483 597 NNLKKQIENKNKNIEELHQENKALKKKGSAENKQLN 632
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
157-481 |
1.89e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 157 LKCSKEEKLSLTKSLDDVTRQLHITQETLSEKMQELDKLRSEwaSHTAALTNKHSQELTNEKEKALQTQVQYQQQHEQQK 236
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE--LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 237 KDLEAlhqrNIHQLQNRLSELEAANKELterkykgDSTVRELKAKLAGVEEELQRTKQEVLSLRREnctldtechekekh 316
Cdd:TIGR04523 387 KNLES----QINDLESKIQNQEKLNQQK-------DEQIKKLQQEKELLEKEIERLKETIIKNNSE-------------- 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 317 INQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKT 396
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 397 LMGKLKLKNTVTIQQEKLLAEKEEMLQK--ERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWL 474
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDELNKddFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
....*..
gi 564338581 475 NKELNEN 481
Cdd:TIGR04523 602 IKEIEEK 608
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
236-480 |
2.71e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 236 KKDLEALHQRNIHQLQNRLSELEAANKELTERKYKgDSTVRELKAKLAGVEEELQRTKQEVLSLRRENC----------- 304
Cdd:PRK01156 503 KKRKEYLESEEINKSINEYNKIESARADLEDIKIK-INELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWlnalavislid 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 305 --TLDTECHEKEKHINQLQTKVAVLEQEIKD----KDQLVLRTKEAFDTIQEQKVALEENgeknQIQLGKLEATIKSLSA 378
Cdd:PRK01156 582 ieTNRSRSNEIKKQLNDLESRLQEIEIGFPDdksyIDKSIREIENEANNLNNKYNEIQEN----KILIEKLRGKIDNYKK 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 379 ELLKANEIIKKlqgdlktlmgklklKNTVTIQqeklLAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLE 458
Cdd:PRK01156 658 QIAEIDSIIPD--------------LKEITSR----INDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRIN 719
|
250 260
....*....|....*....|....
gi 564338581 459 ESKQLLKNNEKLITWLN--KELNE 480
Cdd:PRK01156 720 DINETLESMKKIKKAIGdlKRLRE 743
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
237-402 |
3.54e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 237 KDLEALHQRnIHQLQNRLSELEAANKELteRKYKGDSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKEKH 316
Cdd:COG4913 255 EPIRELAER-YAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 317 INQ--------LQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQ----LGKLEATIKSLSAELLKAN 384
Cdd:COG4913 332 IRGnggdrleqLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEaaalLEALEEELEALEEALAEAE 411
|
170
....*....|....*...
gi 564338581 385 EIIKKLQGDLKTLMGKLK 402
Cdd:COG4913 412 AALRDLRRELRELEAEIA 429
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
163-483 |
3.80e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 163 EKLSLTKSLDDVTRQLHITQETLSEKMQELDKlrsewashtaaltNKHSQELTNEKEKALQTQVQYQQQHEQQKKDLEAL 242
Cdd:pfam02463 660 EKSEVKASLSELTKELLEIQELQEKAESELAK-------------EEILRRQLEIKKKEQREKEELKKLKLEAEELLADR 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 243 HQRNIHQLQNRLSELEAANKELTERKYKGDSTVRELKAKLAgvEEELQRTKQEVLSLRRENCTLDTECHEKEKHINQLQT 322
Cdd:pfam02463 727 VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS--ELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELR 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 323 KVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKtLMGKLK 402
Cdd:pfam02463 805 ALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEE-ELEEQK 883
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 403 LKNTVTIQQEKLLAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQ 482
Cdd:pfam02463 884 LKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNK 963
|
.
gi 564338581 483 L 483
Cdd:pfam02463 964 R 964
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
244-448 |
4.01e-03 |
|
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: 39.79 E-value: 4.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 244 QRNIHQLQNRLSELEAANkELTERKYKGDST---VRELKAKLAGVEEELQRTKQEVLSLRREnctLDTECHEKEKHINQL 320
Cdd:pfam15905 121 SASVASLEKQLLELTRVN-ELLKAKFSEDGTqkkMSSLSMELMKLRNKLEAKMKEVMAKQEG---MEGKLQVTQKNLEHS 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 321 QTKVAVLEQEIKDKDQLVLRTKEAFDTIQE---QKVALEENGEKNQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTL 397
Cdd:pfam15905 197 KGKVAQLEEKLVSTEKEKIEEKSETEKLLEyitELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQ 276
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 564338581 398 MGKLKLK-NTVTIQQEKLLAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQE 448
Cdd:pfam15905 277 IKDLNEKcKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQ 328
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
240-470 |
4.16e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 40.05 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 240 EALHQRnIHQLQNRLSELEAANKELTERKYKGDSTVREL---KAKLAGVEEELQRTKQEVLSLRRENCTLdtechekEKH 316
Cdd:pfam19220 6 ELLRVR-LGEMADRLEDLRSLKADFSQLIEPIEAILRELpqaKSRLLELEALLAQERAAYGKLRRELAGL-------TRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 317 INQLQTKVAVLEQEIkDKDQLVLRTKEAfdTIQEQKVALEEngeknqiqlgkLEATIKSLSAELLKANEIIKKLQGDLKT 396
Cdd:pfam19220 78 LSAAEGELEELVARL-AKLEAALREAEA--AKEELRIELRD-----------KTAQAEALERQLAAETEQNRALEEENKA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564338581 397 LMGKLKlkntvtiQQEKLLAEKEEMLQKERKESQDAgqslrakEQEVCRLQEQLETTVQKLEESKQLLKNNEKL 470
Cdd:pfam19220 144 LREEAQ-------AAEKALQRAEGELATARERLALL-------EQENRRLQALSEEQAAELAELTRRLAELETQ 203
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
236-391 |
4.20e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 38.73 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 236 KKDLEALhQRNIHQLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVE---EELQRTKQEVLSLRRENCTLDTECHE 312
Cdd:pfam13851 32 KEEIAEL-KKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEkdkQSLKNLKARLKVLEKELKDLKWEHEV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 313 KEKHINQLQtkvavleqeiKDKDQLVLRTKEAFDTIQ----------EQKV-ALEENGEKNQIQLGKLeatIKSLSAELL 381
Cdd:pfam13851 111 LEQRFEKVE----------RERDELYDKFEAAIQDVQqktglknlllEKKLqALGETLEKKEAQLNEV---LAAANLDPD 177
|
170
....*....|
gi 564338581 382 KANEIIKKLQ 391
Cdd:pfam13851 178 ALQAVTEKLE 187
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
244-361 |
4.36e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 244 QRNIHQLQNRLSELEAANKELteRKYkgdstVRELKAKLAGVEEELQRTKQEVLSLRREnctLDTEcHEKEKHINQLQTK 323
Cdd:COG2433 405 ERELTEEEEEIRRLEEQVERL--EAE-----VEELEAELEEKDERIERLERELSEARSE---ERRE-IRKDREISRLDRE 473
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 564338581 324 VAVLEQEIKDKDQlvlRTKEAFDTIQEQK--VALEENGEK 361
Cdd:COG2433 474 IERLERELEEERE---RIEELKRKLERLKelWKLEHSGEL 510
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
161-481 |
5.24e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 161 KEEKLSLTKSLDDVTRQLHItqetLSEKMQELDKLRSEWASHTAALTNKHSQELTN--EKEKALQTQVQYQQQHEQQKKD 238
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSV----KELIIKNLDNTRESLETQLKVLSRSINKIKQNleQKQKELKSKEKELKKLNEEKKE 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 239 LEalhqRNIHQLQNRLSELEAANKELTERKYKGDSTVRELKAKL---------AGVEEELQRTKQEVLSLRRENCTLDTE 309
Cdd:TIGR04523 508 LE----EKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkkENLEKEIDEKNKEIEELKQTQKSLKKK 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 310 CHEKEKHINQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATIKSLSAELLKA----NE 385
Cdd:TIGR04523 584 QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIrnkwPE 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 386 IIKKLQgDLKTLMGKLkLKNTVTIQQEKLLAEKEEMLQKERkesqdagqslrakEQEVCRLQEQLETTVQKLEESKQLLK 465
Cdd:TIGR04523 664 IIKKIK-ESKTKIDDI-IELMKDWLKELSLHYKKYITRMIR-------------IKDLPKLEEKYKEIEKELKKLDEFSK 728
|
330
....*....|....*.
gi 564338581 466 NNEKLITWLNKELNEN 481
Cdd:TIGR04523 729 ELENIIKNFNKKFDDA 744
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
161-366 |
5.60e-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: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 161 KEEKLSLTKSLDDVTRQL---HITQETLSEKMQELDKLRSEWASHTAALtNKHSQELTNEKEKALQTQVQYQQQHEQQKK 237
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLnrlTLEKEYLEKEIQELQEQRIDLKEQIKSI-EKEIENLNGKKEELEEELEELEAALRDLES 882
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 238 DLEALhQRNIHQLQNRLSELEAANKELTERKYKGDSTVRELKAKLAGVEEELqrtkQEVLSLRREnctlDTECHEKEKHI 317
Cdd:TIGR02169 883 RLGDL-KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL----SEIEDPKGE----DEEIPEEELSL 953
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 564338581 318 NQLQTKVAVLEQEIKDKDQLVLR-------TKEAFDTIQEQKVALEEngEKNQIQL 366
Cdd:TIGR02169 954 EDVQAELQRVEEEIRALEPVNMLaiqeyeeVLKRLDELKEKRAKLEE--ERKAILE 1007
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
183-483 |
6.49e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 183 ETLSEKMQELDKLRSEWASHTAALTNKHS-QELTNEKEKALQTQVQYQQQHEQQKKDLEAlHQRNIHQLQNRLSELEAAN 261
Cdd:TIGR00606 795 ERFQMELKDVERKIAQQAAKLQGSDLDRTvQQVNQEKQEKQHELDTVVSKIELNRKLIQD-QQEQIQHLKSKTNELKSEK 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 262 KELTERKYKGDSTVRELKAKLAGVEE---ELQRTKQEVLSLRRencTLDTECHEKEKHINQLQTKVAVLEQEIKDK---- 334
Cdd:TIGR00606 874 LQIGTNLQRRQQFEEQLVELSTEVQSlirEIKDAKEQDSPLET---FLEKDQQEKEELISSKETSNKKAQDKVNDIkekv 950
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 335 DQLVLRTKEAFDTIQEQKvaleengeknQIQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNtvtiQQEKL 414
Cdd:TIGR00606 951 KNIHGYMKDIENKIQDGK----------DDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQK----IQERW 1016
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 415 LAEkEEMLQKERKESQDAGQSLRAKEQEVCRLQ-EQLETTVQKLEESKQLLKNNEKLITWLNKELNENQL 483
Cdd:TIGR00606 1017 LQD-NLTLRKRENELKEVEEELKQHLKEMGQMQvLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIK 1085
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
411-482 |
6.86e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.98 E-value: 6.86e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564338581 411 QEKLLAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLITWLNKELNENQ 482
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
317-480 |
6.89e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 317 INQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKN--QIQLGKLEATIKSLSAELlkanEIIKKLQGDL 394
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdEIDVASAEREIAELEAEL----ERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 395 KTLmgklklkntvtiqqekllaekEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESKQLLKNNEKLI-TW 473
Cdd:COG4913 688 AAL---------------------EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLArLE 746
|
....*..
gi 564338581 474 LNKELNE 480
Cdd:COG4913 747 LRALLEE 753
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
244-470 |
9.59e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.00 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 244 QRNIHQLQNRLSELEAANKELTerkykgdSTVRELKAKLAGVEEELQRTKQEVLSLRRENCTLDTECHEKEKHINQLQTK 323
Cdd:pfam01576 804 QAQMKDLQRELEEARASRDEIL-------AQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASG 876
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564338581 324 VAVLEQEIKDKDQLVLRTKEAFDTIQEQKVALEENGEKNQIQLGKLEATI---KSLSAELLKANEIIKKLQGDLKTLMGK 400
Cdd:pfam01576 877 KSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELaaeRSTSQKSESARQQLERQNKELKAKLQE 956
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564338581 401 L------KLKNTVTIQQEKLlAEKEEMLQKERKESQDAGQSLRAKEQEVCRLQEQLETTVQKLEESK-QLLKNNEKL 470
Cdd:pfam01576 957 MegtvksKFKSSIAALEAKI-AQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKdQAEKGNSRM 1032
|
|
| |
