|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
1-825 |
0e+00 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 1164.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 1 MEEESIDLIIKEQKYEELQERLNMELEVNKKINEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQT 80
Cdd:pfam15818 210 MGEENINLTIKEQKFQELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALKENNQT 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 81 LERDNELQREKVKENEEKFLSLEKEHERALGTWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKLCEQKKTEEYKKF 160
Cdd:pfam15818 290 LERDNELQREKVKENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKFEEDKKF 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 161 QNVPELNNENSdELTRKKSENIITQKYNSGPEIWGKNTKSFCLDTEYRE-EEKKDLPVGKT-AEDLQPFEISAKSEINTM 238
Cdd:pfam15818 370 QNVPEVNNENS-EMSTEKSENLIIQKYNSEQEIREENTKSFCSDTEYREtEKKKGPPVEEIiIEDLQVLEKSFKNEIDTS 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 239 VSQDRNQSGMSPHRALCLDKDATDQEQTSDVTDSRKSVTVEVKDKLCLEKASGCSEFKSLNNFFLVVDESLETEMVRLEG 318
Cdd:pfam15818 449 VPQDKNQSEISLSKTLCTDKDLISQGQTLNVTDFRKSVTTEIKDKLCLEKDNGCSEFKSPNNLFLVADQSIETEKIHLES 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 319 TEGLGLLHSggDIPLDTRSNKPSSNGMSNEMAHKRNYNTDGSESNPFKQQSKLLPADLENATEKEITNQDQTKAGLDSFL 398
Cdd:pfam15818 529 TEGLGLHHA--DIHLETESNRSSFNGTLNEMAHNTNHNKDVSENEPFKQQFRLLLCTQENATEKRITNSDQTKAGLDSSL 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 399 DIKLNLDPCKKHGLQDSSHVTLDVKHQKIKQMVREESQCSTEP----RSCYQLASKAPQKPGGTIACAAVVS-PLGPSAS 473
Cdd:pfam15818 607 DVKKNPVQCQKYSLQDSSNVSLDDKQCKIEQLLNKKSECSTLPlkqtSSFQQLCNDTSEKPGLTIPCDTVVShPISPAAF 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 474 SD-KLTALKKSENSINTLPTAAKPAPSPAERTTRTYTNDIQNSSLRNHLGASESSVSVSDFQVNQGDSHTSQAKGLKTVV 552
Cdd:pfam15818 687 SDnLKADLKNSDNNVNIMPMLVKPNSSPGKRTTRKNLDDMQSSQFKNCLGGLENGVTISHLQVNNENSHASQAKDLKTAV 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 553 PLTTSSEKQPPS------ESQITETPKSGLSSLVDVTGRQCMRLNNRDKTEALNGILSGGTCREGQLEEAHLSPATPSAD 626
Cdd:pfam15818 767 HPKTSTEIQFSSkesqidENQITEATKNDLFLLVNVNERQHTLLNNTEKTESLNDIVSGKIYSEGQLEESHSFHIKPSGD 846
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 627 SVSTSARSAFDLPSPD-KPEKTPGYIKFVPPSPWPKVNQT--KTVGTATPSIPLFLKEKTVDLSGSRVTTPVTFCKNVVL 703
Cdd:pfam15818 847 LVNRSGRSAFDLSTSDkKTEKTPVYLNFLDPSPWSKVNQTegQTVSTSTSSIPLLLKEKPIGPSENTKIISVTLCKNVGV 926
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 704 DDTRKNIESDPTSNSRAADTVSNWSIHLDPKGQPREERNATAQTVYDSSFPTEHVKAEPLISTVQQSHSQTVKVTDSPDP 783
Cdd:pfam15818 927 DDVRKDIGPDTTSISRVADTLNNSSIHPDPKGEPSEERNATAKTFYDSSFPTEHVKTEPLKSTVLQSHFQTVKIKDSPDL 1006
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 187956231 784 LTFSPGNNDWQSLVMNRLTEIEKLLSLESDNQPKRRKVEEML 825
Cdd:pfam15818 1007 LKSSPGEDDWQSLITNQITEIEKLLSLENDNQPKKRKAEEML 1048
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-156 |
1.03e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 2 EEESIDLIIKEQKYEELQERLNMELEVNKKINEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTL 81
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187956231 82 ERDNELQREKVKENEEKFLSLEKEHERALGTWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKLCEQKKTEE 156
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
12-247 |
1.18e-05 |
|
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: 49.28 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 12 EQKYEELQERLNM--------ELEVNKKiNEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTLER 83
Cdd:TIGR02168 252 EEELEELTAELQEleekleelRLEVSEL-EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 84 DNELQREKVKENEEKFLSLEKEH-----------------ERALGTWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYN 146
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELesleaeleeleaeleelESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 147 KLCEqkkteeykkfqNVPELNNENSDELTRKKSENIITQKYNSGPEIWGKNTKSFCLDTEYREEEKKDLPVGKTAEDLQP 226
Cdd:TIGR02168 411 RLED-----------RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA 479
|
250 260
....*....|....*....|....
gi 187956231 227 FE---ISAKSEINTMVSQDRNQSG 247
Cdd:TIGR02168 480 AErelAQLQARLDSLERLQENLEG 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-174 |
2.32e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 2 EEESIDLIIKEQKYEELQERLNMELEVNKKINEEITHIQEEKQDIIISFQHMQQLLQQET-------QANTEIDAELKVL 74
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLErriaateRRLEDLEEQIEEL 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 75 RENNQTLE---RDNELQREKVKENEEKFLSLEKEHERALGTWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKLCEQ 151
Cdd:TIGR02168 851 SEDIESLAaeiEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR 930
|
170 180
....*....|....*....|...
gi 187956231 152 KKTEEYKKFQNVPELNNENSDEL 174
Cdd:TIGR02168 931 LEGLEVRIDNLQERLSEEYSLTL 953
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-156 |
3.56e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 2 EEESIDLIIKEQKYEELQERLNMELEVNKKINEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTL 81
Cdd:COG1196 221 ELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL 300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187956231 82 ERDNELQREKVKENEEKFLSLEKEHERalgtWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKLCEQKKTEE 156
Cdd:COG1196 301 EQDIARLEERRRELEERLEELEEELAE----LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2-180 |
5.02e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 2 EEESIDLII--KEQKYEELQERLnmelevnKKINEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQ 79
Cdd:TIGR02169 302 EIASLERSIaeKERELEDAEERL-------AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 80 TLERDNELQREKVKENEEKFLSLEKEHERALGTWKKHVEE---LSGEMNGIKNELSSLRETHAKLQEHYNKLCEQKKTEE 156
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEElqrLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE 454
|
170 180
....*....|....*....|....
gi 187956231 157 YKKFQNVPELNNEnSDELTRKKSE 180
Cdd:TIGR02169 455 WKLEQLAADLSKY-EQELYDLKEE 477
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
11-186 |
6.83e-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: 46.55 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 11 KEQKYEELQERLNMELEVNKKINEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTLERDNELQRE 90
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 91 KVKENEEKFLSLE----------KEHERALGTWKKHVEELSGEMNGIKNELSSL-RETHAKLQEHyNKLCEQKKTEEykk 159
Cdd:TIGR04523 434 TIIKNNSEIKDLTnqdsvkeliiKNLDNTRESLETQLKVLSRSINKIKQNLEQKqKELKSKEKEL-KKLNEEKKELE--- 509
|
170 180
....*....|....*....|....*...
gi 187956231 160 fQNVPELNNENSDELTR-KKSENIITQK 186
Cdd:TIGR04523 510 -EKVKDLTKKISSLKEKiEKLESEKKEK 536
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-180 |
9.00e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 9.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 2 EEESIDLIIKEQKYEELQERLNMELEVNKKINEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTL 81
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 82 ERDNELQREKVKENEEKFLSLEKEHERALGTWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKLCEQKKTEEYKKFQ 161
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
170
....*....|....*....
gi 187956231 162 NvpELNNENSDELTRKKSE 180
Cdd:COG1196 472 A--ALLEAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-183 |
1.02e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 1 MEEESIDLIIKEQKYEELQERLNMELE-VNKKINEEITHIQEEKQDIIISFQHMQQLLQQETQanteIDAELKVLRENNQ 79
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEqLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ----LSKELTELEAEIE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 80 TLERDNELQREKVKENEEKFLSLEKEheralgtwkkhVEELSGEMNGIKNELSSLRETHAKLQEHYNKLceQKKTEEYKK 159
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEAEIEELEAQ-----------IEQLKEELKALREALDELRAELTLLNEEAANL--RERLESLER 831
|
170 180
....*....|....*....|....
gi 187956231 160 FQNVPELNNENSDELTRKKSENII 183
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIE 855
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2-159 |
1.23e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 2 EEESIDLIIKEQKYEELQERL---NMELEVNKKINEEITHIQEEKQDIIISFQHMQQL------LQQETQANTEIDAELK 72
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELeelEEELEELEAELEELREELEKLEKLLQLLPLYQELealeaeLAELPERLEELEERLE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 73 VLRENNQTLERDNELQREKVKENEEKFLSLEKEHERALGTWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKLCEQK 152
Cdd:COG4717 157 ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
....*..
gi 187956231 153 KTEEYKK 159
Cdd:COG4717 237 EAAALEE 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
11-142 |
2.14e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 11 KEQKYEELQERLNmELEVN--------KKINEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTLE 82
Cdd:TIGR02169 362 LKEELEDLRAELE-EVDKEfaetrdelKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE 440
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 83 RDNELQREKVKENEEKFLSLEKEheraLGTWKKHVEELSGEMNGIKNELSSLRETHAKLQ 142
Cdd:TIGR02169 441 EEKEDKALEIKKQEWKLEQLAAD----LSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-156 |
3.57e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 2 EEESIDLIIKEQKYEELQERLNMELEvnkKINEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTL 81
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELE---ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 187956231 82 ERDNELQREKVKENEEKFLSLEKEHERALGTWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKLCEQKKTEE 156
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1-148 |
3.89e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 1 MEEESIDLIIKEQKYEELQERLNMELEVNKKINEEITHIQEEKQDIIisfQHMQQLLQQETQANTEIDAELKVLRENNQT 80
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA---EELLEALRAAAELAAQLEELEEAEEALLER 415
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187956231 81 LERdNELQREKVKENEEKFLSLEKEHERALGTWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKL 148
Cdd:COG1196 416 LER-LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
3-159 |
4.68e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 3 EESIDLIIKE----QKYEELQERLnmeLEVNKKINEEIthiqEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENN 78
Cdd:PRK03918 144 DESREKVVRQilglDDYENAYKNL---GEVIKEIKRRI----ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSEL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 79 QTLERDNELQREKVKENEEKFLSLEkEHERALGTWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKLCE-QKKTEEY 157
Cdd:PRK03918 217 PELREELEKLEKEVKELEELKEEIE-ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElKEKAEEY 295
|
..
gi 187956231 158 KK 159
Cdd:PRK03918 296 IK 297
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
12-115 |
5.39e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.58 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 12 EQKYEELQERLNMELEVNKKINEEITHIQEEKQDIIISfqhmqQLLQQETQANTEIDAELKVLRENNQ---TLERDNELQ 88
Cdd:pfam05557 152 EQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIV-----KNSKSELARIPELEKELERLREHNKhlnENIENKLLL 226
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 187956231 89 REKVK------ENEEKF------LSLEKEH-ERALGTWKK 115
Cdd:pfam05557 227 KEEVEdlkrklEREEKYreeaatLELEKEKlEQELQSWVK 266
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3-185 |
7.42e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 7.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 3 EESIDLIIKEQKYEELQERLNMELEVNKKINEEITHIQEEKQDIIISFQHMQQLLQQETQAnteidaelkvLRENNQTLE 82
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEEN----------LDRKLELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 83 -RDNELQrEKVKENEEKFLSLEKEHERALGTWKKHVEELSgemngiknELSSLRETHAKlQEHYNKLCEQKKTEEYKKFQ 161
Cdd:PRK12704 107 kREEELE-KKEKELEQKQQELEKKEEELEELIEEQLQELE--------RISGLTAEEAK-EILLEKVEEEARHEAAVLIK 176
|
170 180
....*....|....*....|....
gi 187956231 162 NVPELNNENSDeltrKKSENIITQ 185
Cdd:PRK12704 177 EIEEEAKEEAD----KKAKEILAQ 196
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
17-163 |
7.53e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 17 ELQERLNMELEVnkkINEEITHIQEEKQDI--IIsfqhmQQLLQQETQANTEIdAELKVLRENNQTLERDNELQREKVKE 94
Cdd:PRK00409 492 EIAKRLGLPENI---IEEAKKLIGEDKEKLneLI-----ASLEELERELEQKA-EEAEALLKEAEKLKEELEEKKEKLQE 562
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187956231 95 NEEKFLS-LEKEHERALGTWKKHVEELSGEMNGIKNELSS------LRETHAKLQEHYNKLcEQKKTEEYKKFQNV 163
Cdd:PRK00409 563 EEDKLLEeAEKEAQQAIKEAKKEADEIIKELRQLQKGGYAsvkaheLIEARKRLNKANEKK-EKKKKKQKEKQEEL 637
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
12-143 |
8.13e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 12 EQKYEELQERLNmelEVNKKINEEITHIQEEKQDIIIsfqhmQQLLQQETQANTEIDAELKVLRENN---QTLERD-NEL 87
Cdd:COG3206 232 RAELAEAEARLA---ALRAQLGSGPDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNHpdvIALRAQiAAL 303
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 187956231 88 QREKVKENEEKFLSLEKEHERAlgtwKKHVEELSGEMNGIKNELSSLRETHAKLQE 143
Cdd:COG3206 304 RAQLQQEAQRILASLEAELEAL----QAREASLQAQLAQLEARLAELPELEAELRR 355
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
3-159 |
8.75e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 8.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 3 EESIDLIIKEQKYEELQERLNMELEVNKKINEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKvlrennqtlE 82
Cdd:COG1340 133 EEEKELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYK---------E 203
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 187956231 83 RDNelQREKVKENEEKFLSLEKEheralgtwkkhVEELSGEMNGIKNELSSLRETHAKLQEHYNKLCEQKKTEEYKK 159
Cdd:COG1340 204 ADE--LRKEADELHKEIVEAQEK-----------ADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEE 267
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
17-148 |
9.70e-04 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 42.02 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 17 ELQERLNMELEvnkkinEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLrennQTLERDNELqREKVKENE 96
Cdd:COG4026 73 ELAEKFFEELK------GMVGHVERMKLPLGHDVEYVDVELVRKEIKNAIIRAGLKSL----QNIPEYNEL-REELLELK 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 187956231 97 EKFLSLEKEHERALgtwkKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKL 148
Cdd:COG4026 142 EKIDEIAKEKEKLT----KENEELESELEELREEYKKLREENSILEEEFDNI 189
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
3-187 |
1.29e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 3 EESIDLIIKEQKYEELQERLnmeLEVNKKINEEITHIQEEKQDIIISFQHMQQLLQQETQA-------NTEIDAELKVLR 75
Cdd:TIGR00618 283 QERINRARKAAPLAAHIKAV---TQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIeeqrrllQTLHSQEIHIRD 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 76 ENNQTLERDNELQREKVKENEEKFLSLEKEH-ERALGTWKKHVEELSGEMNGIKNELSSLR---------ETHAKLQEHY 145
Cdd:TIGR00618 360 AHEVATSIREISCQQHTLTQHIHTLQQQKTTlTQKLQSLCKELDILQREQATIDTRTSAFRdlqgqlahaKKQQELQQRY 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 187956231 146 NKLCEQKKTEEYK-KFQNVPELNN--ENSDELTRK-KSENIITQKY 187
Cdd:TIGR00618 440 AELCAAAITCTAQcEKLEKIHLQEsaQSLKEREQQlQTKEQIHLQE 485
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
3-148 |
1.44e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 3 EESIDLIIKEQKYEELQERLnmelevnkkINEEIThiqEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTLE 82
Cdd:COG2433 366 DEVKARVIRGLSIEEALEEL---------IEKELP---EEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE 433
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 187956231 83 RDNELQREKVKENEEKfLSLEKEHERALGTWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKL 148
Cdd:COG2433 434 AELEEKDERIERLERE-LSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-183 |
1.58e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 1 MEEESIDLIIKEQKYEELQERLNMEL---------EVNKKInEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAEL 71
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELeelgfesveELEERL-KELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAF 632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 72 KVLRENNQTLE----RDNELQR----EKVKENEEKFLSLEKEHERA---LGTWKKHVEELS----------GEMNGIKNE 130
Cdd:PRK03918 633 EELAETEKRLEelrkELEELEKkyseEEYEELREEYLELSRELAGLraeLEELEKRREEIKktleklkeelEEREKAKKE 712
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 187956231 131 LSSLRETHAKLQEHYNKLCEQKKTEEYKKFQNVPELNNENSDELTRKKSENII 183
Cdd:PRK03918 713 LEKLEKALERVEELREKVKKYKALLKERALSKVGEIASEIFEELTEGKYSGVR 765
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
56-151 |
1.58e-03 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 39.91 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 56 LLQQETQANTEIDAELKVLRENNQTLERDNELQREKVKENEEKFLSLEKEHERALGTWKKHVEELSGEMNGIKNE-LSSL 134
Cdd:pfam09744 37 LLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEELEEIEDQWEQETKDLLSQVESLEEENRRLEADhVSRL 116
|
90
....*....|....*..
gi 187956231 135 RETHAKLQEHYNKLCEQ 151
Cdd:pfam09744 117 EEKEAELKKEYSKLHER 133
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
13-172 |
1.67e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 41.41 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 13 QKYEELQERLNMELEVNKKINEEITHIQEEKQDIiisfqhMQQLLQQEtQANTEIDAELKVLRENNQTLERDNELQREKV 92
Cdd:cd16269 149 EDREKLVEKYRQVPRKGVKAEEVLQEFLQSKEAE------AEAILQAD-QALTEKEKEIEAERAKAEAAEQERKLLEEQQ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 93 KENEEKFLSLEKEHEralgtwkKHVEELSGEMngiKNELSSLRETHAKLQEHynKLCEQKKTEEYKKFQNVPELNNENSD 172
Cdd:cd16269 222 RELEQKLEDQERSYE-------EHLRQLKEKM---EEERENLLKEQERALES--KLKEQEALLEEGFKEQAELLQEEIRS 289
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
12-135 |
1.72e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.76 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 12 EQKYEELQERLNMELEVNKKINEEITHIQE---------------EKQ--DIIISFQHMQQLLQQETQANTEIDAELKVL 74
Cdd:pfam06160 290 EKNLPEIEDYLEHAEEQNKELKEELERVQQsytlnenelervrglEKQleELEKRYDEIVERLEEKEVAYSELQEELEEI 369
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 187956231 75 RENNQTLErdnelqrEKVKENEEKFLSLEKEHERAlgtwKKHVEELSGEMNGIKNELSSLR 135
Cdd:pfam06160 370 LEQLEEIE-------EEQEEFKESLQSLRKDELEA----REKLDEFKLELREIKRLVEKSN 419
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
11-242 |
2.75e-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: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 11 KEQKYEELQERLNMELEVNKKINEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKvlrENNQTLERDNELQRE 90
Cdd:TIGR04523 209 KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS---EKQKELEQNNKKIKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 91 KVKE-----------NEEKFLSLEKEHERALGTWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKLC--EQKKTEEY 157
Cdd:TIGR04523 286 LEKQlnqlkseisdlNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSEseNSEKQREL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 158 KKFQN-VPELNNENSDELtrKKSENIITQKYNSGPEIWGKNTKSFCLDTEYREEEKKDLPVGKTAEDLQPFEISAKSEIN 236
Cdd:TIGR04523 366 EEKQNeIEKLKKENQSYK--QEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIK 443
|
....*.
gi 187956231 237 TMVSQD 242
Cdd:TIGR04523 444 DLTNQD 449
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
4-166 |
5.62e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 4 ESIDLIIKEQkyEELQERLNMELEVNKKINEEiTHIQEEKQDIIISFQ----HMQQLLQQETQANTEIDAELKVLRENNQ 79
Cdd:TIGR00618 584 EDIPNLQNIT--VRLQDLTEKLSEAEDMLACE-QHALLRKLQPEQDLQdvrlHLQQCSQELALKLTALHALQLTLTQERV 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 80 T----LERDNELQREKVKENEEKFL------------------SLEKEHERALGTWKKHVEELSGEMNGIKNELSSLRET 137
Cdd:TIGR00618 661 RehalSIRVLPKELLASRQLALQKMqsekeqltywkemlaqcqTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDA 740
|
170 180 190
....*....|....*....|....*....|
gi 187956231 138 HAKLQEHYNKLC-EQKKTEEYKKFQNVPEL 166
Cdd:TIGR00618 741 LNQSLKELMHQArTVLKARTEAHFNNNEEV 770
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1-159 |
6.55e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 1 MEEESIDLIIKEQKyEELQERLNMELEVNKKI---NEEITHIQEEKQDIiisfQHMQQLLQQETQANTEIDAELKVLREN 77
Cdd:PRK03918 186 KRTENIEELIKEKE-KELEEVLREINEISSELpelREELEKLEKEVKEL----EELKEEIEELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 78 NQTLERDNELQREKVKENEEKFLSLE--KEHERALGTWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKLCEQK-KT 154
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEeRL 340
|
....*
gi 187956231 155 EEYKK 159
Cdd:PRK03918 341 EELKK 345
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
11-180 |
6.96e-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: 39.75 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 11 KEQKYEELQERLNMELEVNKKINEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTLERDNELQRE 90
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 91 KVKE-----------NEEKFL---SLEKEHERALGTWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKLcEQKKTEE 156
Cdd:COG4942 105 ELAEllralyrlgrqPPLALLlspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL-EALLAEL 183
|
170 180
....*....|....*....|....
gi 187956231 157 YKKFQNVPELNNENSDELTRKKSE 180
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKE 207
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
4-106 |
7.13e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 39.89 E-value: 7.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 4 ESIDLIIKEQkyEELQERLNMeLEVN-KKINEEITHIQEEKQDIIISFQHMQQLLQQ-------ETQANTEIDAELKVLR 75
Cdd:PLN02939 156 EDLEKILTEK--EALQGKINI-LEMRlSETDARIKLAAQEKIHVEILEEQLEKLRNEllirgatEGLCVHSLSKELDVLK 232
|
90 100 110
....*....|....*....|....*....|....
gi 187956231 76 ENNQTLERDNELQREK---VKENEEKFLSLEKEH 106
Cdd:PLN02939 233 EENMLLKDDIQFLKAElieVAETEERVFKLEKER 266
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
15-158 |
9.67e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 38.85 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 187956231 15 YEELQERLNMELEVNKKINEEITHIQEEKQDIIISFQHMQ----QLLQQETQANTEIDAELKVLRENNQTLERDNELQRE 90
Cdd:smart00787 146 KEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEeelrQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVK 225
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 187956231 91 KVKENEEKFLSLEKEheralgtwkkhVEELSGEMNGIKNELSSLRETHAKlqehyNKLCEQKKTEEYK 158
Cdd:smart00787 226 KLEELEEELQELESK-----------IEDLTNKKSELNTEIAEAEKKLEQ-----CRGFTFKEIEKLK 277
|
|
| |
