|
Name |
Accession |
Description |
Interval |
E-value |
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
29-355 |
1.08e-11 |
|
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: 69.28 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 29 ELEEATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEIKRAEDLCRLMKEKLEEEENLtreLKS 108
Cdd:TIGR04523 350 ELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL---LEK 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 109 EIERLQkrmAELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKELESSedrLDKTEQSLASELEKLKS 188
Cdd:TIGR04523 427 EIERLK---ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN---LEQKQKELKSKEKELKK 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 189 LTlsfvSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLRIEDGISSTLPSKESRRKGG-LDYLKQ- 266
Cdd:TIGR04523 501 LN----EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKeIEELKQt 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 267 VENETRNKSENEKNRNQEDNKVKDLNQEIEKLKTQIkhfESLEEELKKMKSKNNDLQDNYLSEQNKNKLLASQLEEIKLQ 346
Cdd:TIGR04523 577 QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI---SSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKET 653
|
....*....
gi 2065208820 347 IKKQKELEN 355
Cdd:TIGR04523 654 IKEIRNKWP 662
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8-283 |
2.80e-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: 68.16 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 8 KETASSRHLRFKLQSLSRRLDE-LEEATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEIkrAE 86
Cdd:TIGR02168 246 EELKEAEEELEELTAELQELEEkLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEEL--EA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 87 DLCRLMKEKLEEEENLTR------ELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLTKK----ISSELE 156
Cdd:TIGR02168 324 QLEELESKLDELAEELAEleekleELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELqiasLNNEIE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 157 MLRvkvKELESSEDRLDKTEQSLASELEKLKSLTLSFVSERkyLNEKEKENEKLIKELTQKLEQNKKmnrdytrnASNLE 236
Cdd:TIGR02168 404 RLE---ARLERLEDRRERLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEALEE--------LREEL 470
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2065208820 237 RNDLRIEDGISSTLPSKESRRKGGLDYLKQVENETRNKSENEKNRNQ 283
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
54-363 |
9.67e-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: 66.23 E-value: 9.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 54 AEGSNSSMLA---EIEVLRQRVLRIEGKDEEIKRAEDlcrlmkekleeeenltrELKSEIERLQKRMAELEKLEEAFSRS 130
Cdd:TIGR02168 665 SAKTNSSILErrrEIEELEEKIEELEEKIAELEKALA-----------------ELRKELEELEEELEQLRKELEELSRQ 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 131 KNDC-TQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLASELEKLKSLTlsfvSERKYLNEKEKENEK 209
Cdd:TIGR02168 728 ISALrKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE----AQIEQLKEELKALRE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 210 LIKELTQKLEQNKKMNRDYTRNASNLERNDLRIEDGISSTLPSKESRRKGGLDYLKQVENETRNKSENEKNRNQEDNKVK 289
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERA 883
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2065208820 290 DLNQEIEKLKtqiKHFESLEEELKKMKSKNNDLQDNYLSEQNKNKLLASQLEEIKLQIKKQKE--LENGEVEGEDA 363
Cdd:TIGR02168 884 SLEEALALLR---SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQErlSEEYSLTLEEA 956
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
104-361 |
1.78e-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: 65.46 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 104 RELKSEIERLQKRMA--ELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLAS 181
Cdd:TIGR02168 216 KELKAELRELELALLvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 182 ELEKLKsltlsfvSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLRIEDGISStLPSKESRRKGGL 261
Cdd:TIGR02168 296 EISRLE-------QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES-LEAELEELEAEL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 262 DYLKQVENETRNKSENEKNR-NQEDNKVKDLNQEIEKLKTQIkhfESLEEELKKMKSKNNDLQDNyLSEQNKNKLLASQL 340
Cdd:TIGR02168 368 EELESRLEELEEQLETLRSKvAQLELQIASLNNEIERLEARL---ERLEDRRERLQQEIEELLKK-LEEAELKELQAELE 443
|
250 260
....*....|....*....|.
gi 2065208820 341 EEIKLQIKKQKELENGEVEGE 361
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALE 464
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
30-362 |
3.10e-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: 64.27 E-value: 3.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 30 LEEATKNLQKAEDELLDLQDKviQAEGSNSSMLAEIEVLRQRVLRIEGK-DEEIKRAEDLCRLMKEKLEEEENLTRELKS 108
Cdd:TIGR04523 283 IKELEKQLNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKLEEIQNQiSQNNKIISQLNEQISQLKKELTNSESENSE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 109 EIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKteqslasELEKLKS 188
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK-------EIERLKE 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 189 LTLSFVSERKYLNEKEKENEKLIKEL---TQKLEQN-KKMNRDYTRNASNLERNDLRIEDGIS--STLPSKESRRKGGLD 262
Cdd:TIGR04523 434 TIIKNNSEIKDLTNQDSVKELIIKNLdntRESLETQlKVLSRSINKIKQNLEQKQKELKSKEKelKKLNEEKKELEEKVK 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 263 YLKQVENETRNKSEN-EKNRNQEDNKVKDLNQEIEK---------LKTQI----KHFESLEEELKKMKSKNNDLQ---DN 325
Cdd:TIGR04523 514 DLTKKISSLKEKIEKlESEKKEKESKISDLEDELNKddfelkkenLEKEIdeknKEIEELKQTQKSLKKKQEEKQeliDQ 593
|
330 340 350
....*....|....*....|....*....|....*..
gi 2065208820 326 YlsEQNKNKLLASQLEEIKLQIKKQKELENGEVEGED 362
Cdd:TIGR04523 594 K--EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
10-353 |
3.19e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 64.70 E-value: 3.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 10 TASSRHLRFKLQSLSRRLDELEEATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEIK------ 83
Cdd:TIGR02169 656 TGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEqeeekl 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 84 --RAEDLCRLMKEKLEEEENLTRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLclSLNEERNLTKKISSELEMLRVK 161
Cdd:TIGR02169 736 keRLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS--RIPEIQAELSKLEEEVSRIEAR 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 162 VKELESSEDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLR 241
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 242 IEDGISStLPSKESRRKGGLDYLKQVENETRNKSENEKNRNQEDNKVKDLNQE-------IEKLKTQIkhfESLEEELKK 314
Cdd:TIGR02169 894 LEAQLRE-LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelsLEDVQAEL---QRVEEEIRA 969
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2065208820 315 MKSKNN-------DLQDNYLSEQNKNKLLASQLEEIKLQIKKQKEL 353
Cdd:TIGR02169 970 LEPVNMlaiqeyeEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
16-324 |
5.50e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.92 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 16 LRFKLQSLSRRLDELEEATKNLQKAEDELldlQDKVIQAEGSNSSMLAEIEVLRQRVLRIEgkdEEIKRAEDLCRLMKEK 95
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEEL---SRQISALRKDLARLEAEVEQLEERIAQLS---KELTELEAEIEELEER 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 96 LEEEENLTRELKSEIERLQKRMAELEKLEEAFSRSKNdctqlclSLNEERNLTK-KISSELEMLRVKVKELESSEDRLDK 174
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD-------ELRAELTLLNeEAANLRERLESLERRIAATERRLED 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 175 TEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDY-----TRNASNLERNDLRIE----DG 245
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELeelseELRELESKRSELRREleelRE 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 246 ISSTLPSKESRRKGGLDYLKQVENE---------TRNKSENEKNRNQEDNKVKDLNQEIEKLK----TQIKHFESLEEEL 312
Cdd:TIGR02168 923 KLAQLELRLEGLEVRIDNLQERLSEeysltleeaEALENKIEDDEEEARRRLKRLENKIKELGpvnlAAIEEYEELKERY 1002
|
330
....*....|..
gi 2065208820 313 KKMKSKNNDLQD 324
Cdd:TIGR02168 1003 DFLTAQKEDLTE 1014
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
21-248 |
7.26e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.55 E-value: 7.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 21 QSLSRRLDELEEATKNLQK-AEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVlriEGKDEEIKRAEDLCRLMKEKLEee 99
Cdd:TIGR02169 265 KRLEEIEQLLEELNKKIKDlGEEEQLRVKEKIGELEAEIASLERSIAEKEREL---EDAEERLAKLEAEIDKLLAEIE-- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 100 eNLTRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSL 179
Cdd:TIGR02169 340 -ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2065208820 180 ASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLRIEDGISS 248
Cdd:TIGR02169 419 SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
28-261 |
1.43e-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: 61.32 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 28 DELEEATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEgkdEEIKRAEDLCRLMKEKLEEEENLTRELK 107
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA---RRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 108 SEIERLQKRMAELekLEEAFSRSKNDCTQLCLS---LNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLASELE 184
Cdd:COG4942 97 AELEAQKEELAEL--LRALYRLGRQPPLALLLSpedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 185 KLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLRIEDGISS----TLPSKESRRKGG 260
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAaaerTPAAGFAALKGK 254
|
.
gi 2065208820 261 L 261
Cdd:COG4942 255 L 255
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
8-362 |
1.57e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 8 KETASSRHLRFKLQSLSRRLDELEEATKNLQKAEDELLDLQDKVIQAEGSNSSM------LAEIEVLRQRVL-RIEGKDE 80
Cdd:PRK03918 249 SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYeeyldeLREIEKRLSRLEeEINGIEE 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 81 EIKRAEDLCRLMkekleeeenltRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQL--------CLSLNEERNLTKKIS 152
Cdd:PRK03918 329 RIKELEEKEERL-----------EELKKKLKELEKRLEELEERHELYEEAKAKKEELerlkkrltGLTPEKLEKELEELE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 153 SELEMLRVKVKELESSEDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENekLIKELTQKLEQNKKMNRDYTRNA 232
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKE--LLEEYTAELKRIEKELKEIEEKE 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 233 SNLERNDLRIEDGISSTlpSKESRRKGGLDYLKQVENETRNKSENEKNRNQED------------NKVKDLNQEIEKLKT 300
Cdd:PRK03918 476 RKLRKELRELEKVLKKE--SELIKLKELAEQLKELEEKLKKYNLEELEKKAEEyeklkekliklkGEIKSLKKELEKLEE 553
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065208820 301 QIKHFESLEEELKKMKSKNNDLQDNYLSEQNKN-KLLASQLEEIKLQIKKQKELENGEVEGED 362
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELGFESvEELEERLKELEPFYNEYLELKDAEKELER 616
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-311 |
1.62e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 3 EFTSYKETASSRHLRFKLQSLSRRLDELEEATKNLQKAEDELLDLQDKVIQAEgsnssmlAEIEVLRQRVLRIEGKDEEI 82
Cdd:COG1196 214 RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELE-------AELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 83 KRAEdlcrlmkekleeeENLTRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKV 162
Cdd:COG1196 287 QAEE-------------YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 163 KELESSEDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLRI 242
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2065208820 243 EDGISSTLPSKESRRKGGLDYLKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEE 311
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
6-355 |
2.20e-09 |
|
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: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 6 SYKETASSRHLRFKlqslsRRLDELEEATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEIKRA 85
Cdd:TIGR04523 23 GYKNIANKQDTEEK-----QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 86 -----EDLCRLMKEKLEEEENLTReLKSEIERLQKRMAELEKLEEAF-SRSKNDCTQLCLSLNEERNLTKKISSELEMLR 159
Cdd:TIGR04523 98 inklnSDLSKINSEIKNDKEQKNK-LEVELNKLEKQKKENKKNIDKFlTEIKKKEKELEKLNNKYNDLKKQKEELENELN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 160 VKVKELESSEDRLDKTEQ--------------------SLASELEKLKS----LTLSFVSERKYLNEKEKENEKLIKELT 215
Cdd:TIGR04523 177 LLEKEKLNIQKNIDKIKNkllklelllsnlkkkiqknkSLESQISELKKqnnqLKDNIEKKQQEINEKTTEISNTQTQLN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 216 QKLEQNKKMNRDYTRNASNLERNDLRIED------GISSTLPSKESRRKGGLD-YLK-QVENETRNKSENEKNRNQEDNK 287
Cdd:TIGR04523 257 QLKDEQNKIKKQLSEKQKELEQNNKKIKElekqlnQLKSEISDLNNQKEQDWNkELKsELKNQEKKLEEIQNQISQNNKI 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2065208820 288 VKDLNQEIEKLKTQIKHFES----LEEELKKMKSKNNDLQDNYLSEQNKNKLLASQLEEIKLQIKKQKELEN 355
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNSESenseKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQ 408
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
28-349 |
2.83e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.23 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 28 DELEEATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEIKRAEDLCRLMKEKLEEEENLTRELK 107
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 108 SEIERLQKRMAELEKLE---EAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLaSELE 184
Cdd:PRK03918 273 KEIEELEEKVKELKELKekaEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL-KELE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 185 KLKSLTLSFVSERKYLNEKEKENEKLIKELTQK-LEQNKKMNRDYTRNASNLERNDLRIEDGISStLPSKESRRKGGLDY 263
Cdd:PRK03918 352 KRLEELEERHELYEEAKAKKEELERLKKRLTGLtPEKLEKELEELEKAKEEIEEEISKITARIGE-LKKEIKELKKAIEE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 264 LKQVENET----RNKSENEKnrnqeDNKVKDLNQEIEKLKTQIKHFESLEEELKKMKsKNNDLQDNYLSEQNKNKLLASQ 339
Cdd:PRK03918 431 LKKAKGKCpvcgRELTEEHR-----KELLEEYTAELKRIEKELKEIEEKERKLRKEL-RELEKVLKKESELIKLKELAEQ 504
|
330
....*....|
gi 2065208820 340 LEEIKLQIKK 349
Cdd:PRK03918 505 LKELEEKLKK 514
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
66-352 |
4.88e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 66 EVLRQRVLRIEGKDEEIKRAEDLcrlmkekleeeENLTRELKSEIERLQKRMAELEKLEEafsrskndctqlclslneer 145
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENI-----------EELIKEKEKELEEVLREINEISSELP-------------------- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 146 nltkKISSELEMLRVKVKELESSEDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKL---------IKELTQ 216
Cdd:PRK03918 218 ----ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELeekvkelkeLKEKAE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 217 KLEQNKKMNRDYTRNASNLERNDLRIEDGIS------STLPSKESRrkggLDYLKQVENETRNKSENEKNRNQEDNKVKD 290
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINgieeriKELEEKEER----LEELKKKLKELEKRLEELEERHELYEEAKA 369
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065208820 291 LNQEIEKLKTQIKHF--ESLEEELKKMKSKNNDLQDNYLSEQNKNKLLASQLEEIKLQIKKQKE 352
Cdd:PRK03918 370 KKEELERLKKRLTGLtpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
63-370 |
9.38e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 9.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 63 AEIEVLRQ--RVLRIEGKDEEIKRAEdlcrlmkekleeeenltRELKSEIERLQKRMAELEKLEEAFSRSKndctqlcLS 140
Cdd:COG1196 220 EELKELEAelLLLKLRELEAELEELE-----------------AELEELEAELEELEAELAELEAELEELR-------LE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 141 LNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQ 220
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 221 NKKMNRDYTRNASNLERNDLRIEDGISSTlpskesrrkggldyLKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKT 300
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEEL--------------AEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 301 QIkhfESLEEELKKMKSKNNDLQDNYLSEQNKNKLLASQLEEIKLQIKKQKELENGEVEGEDAFLSSKGR 370
Cdd:COG1196 422 EL---EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
19-198 |
2.49e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 19 KLQSLSRRLDELEEATKNLQKAEDELLDLQDKVIQAEgsnssmlAEIEVLRQRVLRIEGKDEEIKRAEDLCRLMKEKLEE 98
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELE-------AELEELREELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 99 EENLtRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLC--LSLNEERNLtKKISSELEMLRVKVKELESSEDRLDKTE 176
Cdd:COG4717 145 PERL-EELEERLEELRELEEELEELEAELAELQEELEELLeqLSLATEEEL-QDLAEELEELQQRLAELEEELEEAQEEL 222
|
170 180
....*....|....*....|..
gi 2065208820 177 QSLASELEKLKSLTLSFVSERK 198
Cdd:COG4717 223 EELEEELEQLENELEAAALEER 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
137-370 |
6.27e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 6.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 137 LCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLASELEKLK---SLTLSFVS----ERKYLNEKEKENEK 209
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALErriAALARRIRaleqELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 210 LIKELTQKLEQNKKMNRDYTRNASNLERNDlRIEDGISSTLPSKESRRKGGLDYL-----KQVENETRNKSENEKNRNQE 284
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQP-PLALLLSPEDFLDAVRRLQYLKYLaparrEQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 285 DNKVKDLNQEIEKLKTQIKhfeSLEEELKKMKSKNNDLQDNYLSEQNKNKLLASQLEEIKLQIKK--QKELENGEVEGED 362
Cdd:COG4942 170 EAERAELEALLAELEEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARleAEAAAAAERTPAA 246
|
....*...
gi 2065208820 363 AFLSSKGR 370
Cdd:COG4942 247 GFAALKGK 254
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
19-316 |
6.83e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 19 KLQSLSRRLDELE--EATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEI-KRAEDLCRLMKEK 95
Cdd:TIGR02169 212 RYQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnKKIKDLGEEEQLR 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 96 LEEEenlTRELKSEIERLQKRMAELE-KLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDK 174
Cdd:TIGR02169 292 VKEK---IGELEAEIASLERSIAEKErELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELED 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 175 TEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDytrnASNLERNDLRIEDGISSTLPSKE 254
Cdd:TIGR02169 369 LRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE----LADLNAAIAGIEAKINELEEEKE 444
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2065208820 255 SRRkggldylKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKTQIKhfeSLEEELKKMK 316
Cdd:TIGR02169 445 DKA-------LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS---KLQRELAEAE 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
103-417 |
8.88e-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: 56.61 E-value: 8.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 103 TRELKSEIERLQKRMAELEKLEEafsrskndctqlclSLNEERNltkKISSELEMLRVKVKELESSEDRLDKTEQSLASE 182
Cdd:TIGR02169 669 SRSEPAELQRLRERLEGLKRELS--------------SLQSELR---RIENRLDELSQELSDASRKIGEIEKEIEQLEQE 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 183 LEKLKsltlsfvserkylnEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLRIEDGISStLPSKESRrkggld 262
Cdd:TIGR02169 732 EEKLK--------------ERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND-LEARLSH------ 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 263 ylKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLkTQIKhfESLEEELKKMKSKNNDLQDNYLSEQNKNKLLASQLEE 342
Cdd:TIGR02169 791 --SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL-TLEK--EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2065208820 343 IKLQIKKqKELENGEVEGEDAFLSSkgrhERTKFRGHGSEASVSKHTArELSPQHKRERLRNREFALNNENYSLS 417
Cdd:TIGR02169 866 LEEELEE-LEAALRDLESRLGDLKK----ERDELEAQLRELERKIEEL-EAQIEKKRKRLSELKAKLEALEEELS 934
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
62-347 |
2.39e-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: 55.07 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 62 LAEIEVLRQRVLRIEGKDEEIKRAEDLCRLMKEKLEEEENLTRELK---------------SEIERLQKRMAELEKLEEA 126
Cdd:TIGR02169 176 LEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKReyegyellkekealeRQKEAIERQLASLEEELEK 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 127 FSRSKNDCTQLCLSLNEERN-LTKKIS--SELEMLRVKVK--ELESSEDRLDKTEQSLASELEKLKSLTLSFVSERkylN 201
Cdd:TIGR02169 256 LTEEISELEKRLEEIEQLLEeLNKKIKdlGEEEQLRVKEKigELEAEIASLERSIAEKERELEDAEERLAKLEAEI---D 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 202 EKEKENEKLIKEL-TQKLEQNKKMNR-DYTRNASNLERNDLRIEDGISSTLPSKESRRKGGLDYLKQVENE-TRNKSENE 278
Cdd:TIGR02169 333 KLLAEIEELEREIeEERKRRDKLTEEyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINElKRELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 279 KNRNQEDNKVKDLNQEIEKLKTQIKHFES-----------LEEELKKMKSKNNDLQDNYLSEQNKNKLLASQLEEIKLQI 347
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEekedkaleikkQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
104-354 |
4.80e-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: 54.30 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 104 RELKSEIERLQKRMAELEKLEeAFSRSKNDCTQLCLSLNEERNLT--KKISSELEMLRvkvKELESSEDRLDKTEQSLAS 181
Cdd:TIGR02169 194 DEKRQQLERLRREREKAERYQ-ALLKEKREYEGYELLKEKEALERqkEAIERQLASLE---EELEKLTEEISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 182 ELEKLKSLT--LSFVSERKYLNEKEKeneklIKELTQKLEQNKKMNRDYTRNASNLERNDLRIEDGISSTLPSKESRRKG 259
Cdd:TIGR02169 270 IEQLLEELNkkIKDLGEEEQLRVKEK-----IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 260 GLDYLKQVENETrnkSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMKSKNNDLQDNYLSEQNKNKLLASQ 339
Cdd:TIGR02169 345 IEEERKRRDKLT---EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEE 421
|
250
....*....|....*....
gi 2065208820 340 LEEIKLQIK----KQKELE 354
Cdd:TIGR02169 422 LADLNAAIAgieaKINELE 440
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
13-414 |
5.27e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 54.28 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 13 SRHLRFKLQSLSRRLDELEEATKNLQKAEDELLDLqdkviqAEGSNSSM---LAEIEVLRQRVLRIEGKDEEIKRAEDLC 89
Cdd:TIGR00606 697 ISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGL------APGRQSIIdlkEKEIPELRNKLQKVNRDIQRLKNDIEEQ 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 90 RLMKEKLEEEENLTRELKSEIERLQKRMAELEKLEEAFSR--SKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKELES 167
Cdd:TIGR00606 771 ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQqaAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRK 850
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 168 SEDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLRIEDGIS 247
Cdd:TIGR00606 851 LIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 248 stlpSKESRRKGGLDYLKQVENETRNKSENEK---NRNQE--DNKVKDLNQEIEKLKTQI----KHFESLEEELKKMKSK 318
Cdd:TIGR00606 931 ----SKETSNKKAQDKVNDIKEKVKNIHGYMKdieNKIQDgkDDYLKQKETELNTVNAQLeeceKHQEKINEDMRLMRQD 1006
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 319 --NNDLQDNYLSEQNKNKLLASQLEEIKLQIKKQkeleNGEVeGEDAFLSSKGRH----ERTKFRGHGSEASVSKHTARE 392
Cdd:TIGR00606 1007 idTQKIQERWLQDNLTLRKRENELKEVEEELKQH----LKEM-GQMQVLQMKQEHqkleENIDLIKRNHVLALGRQKGYE 1081
|
410 420
....*....|....*....|..
gi 2065208820 393 LSPQHKRERLRNREFALNNENY 414
Cdd:TIGR00606 1082 KEIKHFKKELREPQFRDAEEKY 1103
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
8-362 |
9.79e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 9.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 8 KETASSRHLRFKLQSLSRRLDELEEATKNLQKaedELLDLQDKviqaegsNSSMLAEIEVLRQRvlrIEGKDEEIKRAED 87
Cdd:TIGR04523 187 KNIDKIKNKLLKLELLLSNLKKKIQKNKSLES---QISELKKQ-------NNQLKDNIEKKQQE---INEKTTEISNTQT 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 88 lcrlmkekleEEENLTRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNE-----ERNLTKKISSELEMlrvKV 162
Cdd:TIGR04523 254 ----------QLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDlnnqkEQDWNKELKSELKN---QE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 163 KELESSEDRLDKTEQSLASELEKLKSLtlsfvseRKYLNEKEKENEKLIKELTQKLEQNKKMNRDytrNASNLERndlri 242
Cdd:TIGR04523 321 KKLEEIQNQISQNNKIISQLNEQISQL-------KKELTNSESENSEKQRELEEKQNEIEKLKKE---NQSYKQE----- 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 243 edgisstlpskesrrkggLDYLKQVENETRNKSENEKNRNQE-DNKVKDLNQEIEKLKTQIkhfesleEELKKMKSKNND 321
Cdd:TIGR04523 386 ------------------IKNLESQINDLESKIQNQEKLNQQkDEQIKKLQQEKELLEKEI-------ERLKETIIKNNS 440
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2065208820 322 LQDNYLSEQNKNKLLASQLEEIKLQIKKQKELENGEVEGED 362
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIK 481
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
78-331 |
1.13e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 78 KDEEIKRAEDLCRLMKEKLEEEEnltRELKSEIERLQKRMAELEKLEEAFSR---SKNDCTQLCLSLNEERNLTKKISSE 154
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKA---EEDKKKAEEAKKAEEDEKKAAEALKKeaeEAKKAEELKKKEAEEKKKAEELKKA 1724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 155 LEMLRVKVKELESSEDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDytRNASN 234
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD--KKIKD 1802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 235 LERNDLRIEDGISSTLP----SKE---SRRKGGLDYLKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFES 307
Cdd:PTZ00121 1803 IFDNFANIIEGGKEGNLvindSKEmedSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEE 1882
|
250 260
....*....|....*....|....
gi 2065208820 308 LEEELKKMKSKNNDLQDNYLSEQN 331
Cdd:PTZ00121 1883 EIEEADEIEKIDKDDIEREIPNNN 1906
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
28-359 |
3.17e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 3.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 28 DELEEATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEIK-RAEDLcrlmkeKLEEEENLTREL 106
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKsEISDL------NNQKEQDWNKEL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 107 KSEIERLQKRMAELE----KLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLASE 182
Cdd:TIGR04523 313 KSELKNQEKKLEEIQnqisQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 183 LEKLKSLTLSFVSERKYLNEK----EKENEKLIKELTQKLEQNKKMNRDYtrnaSNLERNDLRIEDGISSTLPSKESRRK 258
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQikklQQEKELLEKEIERLKETIIKNNSEI----KDLTNQDSVKELIIKNLDNTRESLET 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 259 ggldYLKQVENETRNKSENEKNRNQEdnkVKDLNQEIEKLKTQIKHFESLEEELKKMKSKNNDLQDNYLSEQNKNKLLAS 338
Cdd:TIGR04523 469 ----QLKVLSRSINKIKQNLEQKQKE---LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKIS 541
|
330 340
....*....|....*....|.
gi 2065208820 339 QLEEIKLQIKKQKELENGEVE 359
Cdd:TIGR04523 542 DLEDELNKDDFELKKENLEKE 562
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
19-221 |
3.86e-06 |
|
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: 49.15 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 19 KLQSLSRRLDELEEATKNLQKaedELLDLQDKVIQAEgsnssmlAEIEVLRQrvlRIEGKDEEIKRAEdlcrlmkeklee 98
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPA---ELAELEDELAALE-------ARLEAAKT---ELEDLEKEIKRLE------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 99 eeNLTRELKSEIERLQKRMAELEKLEEAFSRSKndctqlclslnEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQS 178
Cdd:COG1579 66 --LEIEEVEARIKKYEEQLGNVRNNKEYEALQK-----------EIESLKRRISDLEDEILELMERIEELEEELAELEAE 132
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2065208820 179 LASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQN 221
Cdd:COG1579 133 LAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
43-354 |
6.70e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.50 E-value: 6.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 43 ELLDLQDKVIQAEGSNSSMLAEIE-VLRQRVLRIEGKDEEIKRAedlcrlmkekleeeENLTRELKSEIERLQKRMAELE 121
Cdd:pfam15921 420 ELDDRNMEVQRLEALLKAMKSECQgQMERQMAAIQGKNESLEKV--------------SSLTAQLESTKEMLRKVVEELT 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 122 KLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVkELESSEdrldktEQSLASELEKLKSLTlsfvSERKYLN 201
Cdd:pfam15921 486 AKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV-DLKLQE------LQHLKNEGDHLRNVQ----TECEALK 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 202 EKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLRIEDGISStlpskesrRKGGLDYLKQVENETRNKSENEKNR 281
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIND--------RRLELQEFKILKDKKDAKIRELEAR 626
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 282 --NQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMKSKNNDLqdNYLSE---------QNKNKLLASQLEEIKLQIKK- 349
Cdd:pfam15921 627 vsDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNEL--NSLSEdyevlkrnfRNKSEEMETTTNKLKMQLKSa 704
|
....*
gi 2065208820 350 QKELE 354
Cdd:pfam15921 705 QSELE 709
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
19-362 |
9.41e-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: 49.97 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 19 KLQSLSRRLDELEEATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEIKRAEDLCRLMKEKLEE 98
Cdd:pfam02463 723 LADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEE 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 99 EENLTRELKSEIERLQKRMAELEKLEEAFSrskndctqlclSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQS 178
Cdd:pfam02463 803 LRALEEELKEEAELLEEEQLLIEQEEKIKE-----------EELEELALELKEEQKLEKLAEEELERLEEEITKEELLQE 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 179 LASELEKLKSLTLSFVSERKYLNEKEKENEKLiKELTQKLEQNKKMNRDYTRNASNLERNDLRIEDGISSTLPSKESrrk 258
Cdd:pfam02463 872 LLLKEEELEEQKLKDELESKEEKEKEEKKELE-EESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADE--- 947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 259 ggLDYLKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMKSKNNDLQDNYLSEQNKNK-LLA 337
Cdd:pfam02463 948 --KEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEfLEL 1025
|
330 340
....*....|....*....|....*
gi 2065208820 338 SQLEEIKLQIKKQKELENGEVEGED 362
Cdd:pfam02463 1026 FVSINKGWNKVFFYLELGGSAELRL 1050
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
25-318 |
1.08e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 25 RRLDELEEATKNLQKAEDELLDLQDKVIQAEGSnssmlaEIEVLRQRVLRIEGK----DEEIKRAEDLcrlmkekleeeE 100
Cdd:PRK03918 493 SELIKLKELAEQLKELEEKLKKYNLEELEKKAE------EYEKLKEKLIKLKGEikslKKELEKLEEL-----------K 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 101 NLTRELKSEIERLQKRMAELEKleeafsrskndctqlclslneerNLTKKISSELEMLRVKVKELESSEDR---LDKTEQ 177
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLK-----------------------ELEELGFESVEELEERLKELEPFYNEyleLKDAEK 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 178 SLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTqklEQNKKMNRDYTRNASNLERNdlriedgISSTLPSKESRR 257
Cdd:PRK03918 613 ELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE---ELEKKYSEEEYEELREEYLE-------LSRELAGLRAEL 682
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065208820 258 KGGLDYLKQVENETRNKSENEKNRnqednkvKDLNQEIEKLKTQIKHFESLEEELKKMKSK 318
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEER-------EKAKKELEKLEKALERVEELREKVKKYKAL 736
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
22-414 |
1.16e-05 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 48.92 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 22 SLSRRLDELEEATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEIKRaedlcrlmkekleEEEN 101
Cdd:pfam04108 1 SLSSAQDLCRWANELLTDARSLLEELVVLLAKIAFLRRGLSVQLANLEKVREGLEKVLNELKK-------------DFKQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 102 LTRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLS--LNEE--RNLTKKISSELEMLRVKVKELESSEDRLDKTEQ 177
Cdd:pfam04108 68 LLKDLDAALERLEETLDKLRNTPVEPALPPGEEKQKTLLdfIDEDsvEILRDALKELIDELQAAQESLDSDLKRFDDDLR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 178 SLASELEKLKSLTLSFVSERKYLnekeKENEKLIKELTQKLEqnkKMNRDYtrnasnlerndlrieDGISSTLPSKESRR 257
Cdd:pfam04108 148 DLQKELESLSSPSESISLIPTLL----KELESLEEEMASLLE---SLTNHY---------------DQCVTAVKLTEGGR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 258 KGGLDYLKQVENETRNKSENEKNRnqednkVKDLNQEIEKLKTQIKHFESLEEELKKMKSKNNDLQDNYLSEQNKNKLLA 337
Cdd:pfam04108 206 AEMLEVLENDARELDDVVPELQDR------LDEMENNYERLQKLLEQKNSLIDELLSALQLIAEIQSRLPEYLAALKEFE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 338 SQLEEIKLQIKKQKELENGEVEGEDAFLSSKG------RHERT---KFRGHGSEAsvskhtARELSPQHKRERLRNREFA 408
Cdd:pfam04108 280 ERWEEEKETIEDYLSELEDLREFYEGFPSAYGslllevERRREwaeKMKKILRKL------AEELDRLQEEERKRREKFL 353
|
....*.
gi 2065208820 409 LNNENY 414
Cdd:pfam04108 354 KEVGDF 359
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
114-355 |
1.18e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 49.58 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 114 QKRMAELEKLEEafsrskndctqlclslnEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLASELEKLKSLTLsf 193
Cdd:pfam02463 169 RKKKEALKKLIE-----------------ETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYL-- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 194 vserKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNdLRIEDGISSTLPSKESRRKGGLDYLKQVENE--- 270
Cdd:pfam02463 230 ----DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQV-LKENKEEEKEKKLQEEELKLLAKEEEELKSEllk 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 271 ---TRNKSENEKNRNQEDNKVKDlnQEIEKLKTQIKHFESLEEELKKMKSKNNDLQDNY-----LSEQNKNKLLASQLEE 342
Cdd:pfam02463 305 lerRKVDDEEKLKESEKEKKKAE--KELKKEKEEIEELEKELKELEIKREAEEEEEEELeklqeKLEQLEEELLAKKKLE 382
|
250
....*....|...
gi 2065208820 343 IKLQIKKQKELEN 355
Cdd:pfam02463 383 SERLSSAAKLKEE 395
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
28-344 |
1.21e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 49.66 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 28 DELEEATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEIKRAEDLcrlmkekleeEENLTReLK 107
Cdd:TIGR00606 577 DWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE----------ESDLER-LK 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 108 SEIERLQKRMAELEKLEEAFSR-------SKNDCTQLCLSLNEERNLTKKISSELE-MLRVKVKELESSEdrldkteqSL 179
Cdd:TIGR00606 646 EEIEKSSKQRAMLAGATAVYSQfitqltdENQSCCPVCQRVFQTEAELQEFISDLQsKLRLAPDKLKSTE--------SE 717
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 180 ASELEKLKSLTLSFVSERkylnekEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLRIEdgissTLPSKESRRKG 259
Cdd:TIGR00606 718 LKKKEKRRDEMLGLAPGR------QSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG-----TIMPEEESAKV 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 260 GLDYLKQVENETRNKSENEKNRNQEDNKVK--DLNQEIEKLKTQIkhfESLEEELKKMKSKNNDLQDNYLSEQNKNKLLA 337
Cdd:TIGR00606 787 CLTDVTIMERFQMELKDVERKIAQQAAKLQgsDLDRTVQQVNQEK---QEKQHELDTVVSKIELNRKLIQDQQEQIQHLK 863
|
....*..
gi 2065208820 338 SQLEEIK 344
Cdd:TIGR00606 864 SKTNELK 870
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-326 |
1.40e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 2 AEFTSYKETASSRhlRFKLQSLSRRLDELEEATKN----LQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRV----- 72
Cdd:PRK02224 370 SELEEAREAVEDR--REEIEELEEEIEELRERFGDapvdLGNAEDFLEELREERDELREREAELEATLRTARERVeeaea 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 73 LRIEGK----DEEIKRAEDLCRLMKEKLEEEEnLTREL---KSEIERLQKRMAELEKLEEA---FSRSKNDCTQLCLSLN 142
Cdd:PRK02224 448 LLEAGKcpecGQPVEGSPHVETIEEDRERVEE-LEAELedlEEEVEEVEERLERAEDLVEAedrIERLEERREDLEELIA 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 143 EERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKL------------ 210
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIrtllaaiadaed 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 211 -IKELTQKLEQNKKMN---RDYTRNASnlERNDLRIEDGISSTLPSKESRRKGGLDYLKQVENETRNKSEneknrnQEDn 286
Cdd:PRK02224 607 eIERLREKREALAELNderRERLAEKR--ERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELRE------ERD- 677
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2065208820 287 kvkDLNQEIEKLKTQIKHFESLEEELKKMKSKNNDLQDNY 326
Cdd:PRK02224 678 ---DLQAEIGAVENELEELEELRERREALENRVEALEALY 714
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
80-355 |
1.41e-05 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 48.52 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 80 EEIKRAEDLCRLMKEKLEEEENLTRELKSEIERLQ----KRMAELEKLEEAFSrsknDCTQLCLSLneernltkkiSSEL 155
Cdd:pfam15742 20 QNLQRLQILCTSAEKELRYERGKNLDLKQHNSLLQeeniKIKAELKQAQQKLL----DSTKMCSSL----------TAEW 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 156 EMLRVKVKELE-----SSEDRldKTEQSLASELEKLKS-----------------------LTLSFVSERKYLNEKEKE- 206
Cdd:pfam15742 86 KHCQQKIRELElevlkQAQSI--KSQNSLQEKLAQEKSrvadaeekilelqqklehahkvcLTDTCILEKKQLEERIKEa 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 207 --NEKLIKELTQKLEQNKKMnRDYTRNASNLERNDLRIEDGISSTLPSKESRRKGGLD-YLKQVENETRNKSENEKNRNQ 283
Cdd:pfam15742 164 seNEAKLKQQYQEEQQKRKL-LDQNVNELQQQVRSLQDKEAQLEMTNSQQQLRIQQQEaQLKQLENEKRKSDEHLKSNQE 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2065208820 284 EDNKVKDLNQEIEKLKTQIKHF-ESLEEELKKMKSKNNdlqdnylseQNKNKLLASQ---LEEIKLQIKKQKELEN 355
Cdd:pfam15742 243 LSEKLSSLQQEKEALQEELQQVlKQLDVHVRKYNEKHH---------HHKAKLRRAKdrlVHEVEQRDERIKQLEN 309
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
104-363 |
1.72e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 104 RELKSEIERLQKRMA--ELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLAS 181
Cdd:COG1196 216 RELKEELKELEAELLllKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 182 ELEKLKsltlsfvserkylnEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLRIEDGISSTLPSKESRRkggl 261
Cdd:COG1196 296 ELARLE--------------QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE---- 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 262 dylKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMKSKNNDLQDNYLSEQNKNKLLASQLE 341
Cdd:COG1196 358 ---AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260
....*....|....*....|..
gi 2065208820 342 EIKLQIKKQKELENGEVEGEDA 363
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEE 456
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
62-354 |
3.16e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 3.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 62 LAEIEVLRQRVLRIEGKDEEIKRAEDlcrlmKEKLEEEENLTRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSL 141
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQEL-----KLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 142 NEERNLTKKI---SSELEMLRVKVKELESSEDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKL 218
Cdd:pfam02463 250 QEEIESSKQEiekEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 219 EQNKKMNRDYTRNA-SNLERNDLRIEDGISSTLPS--KESRRKGGLDYLKQVENETRNKSENEKN-----RNQEDNKVKD 290
Cdd:pfam02463 330 LKKEKEEIEELEKElKELEIKREAEEEEEEELEKLqeKLEQLEEELLAKKKLESERLSSAAKLKEeelelKSEEEKEAQL 409
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065208820 291 LNQEIEKLKTQIKHFESLEEELKKMKSKNNDLQDNYLSEQNKNKLLASQLEEIKLQIKKQKELE 354
Cdd:pfam02463 410 LLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
16-365 |
4.36e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.79 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 16 LRFKLQSLSRRLDELE-EATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGK----DEEIKRAEDlcr 90
Cdd:pfam05483 213 MHFKLKEDHEKIQHLEeEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKtklqDENLKELIE--- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 91 lmkekleEEENLTRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLS-------LNEERNLTKKISSEL-------- 155
Cdd:pfam05483 290 -------KKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEkeaqmeeLNKAKAAHSFVVTEFeattcsle 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 156 EMLRVKVKELESSEDRLDKTEQSLASELEKLKSLTlsfvserKYLNEKEKENEKLIKELTQK---LEQNKKMNRdytrna 232
Cdd:pfam05483 363 ELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMT-------KFKNNKEVELEELKKILAEDeklLDEKKQFEK------ 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 233 snlerndlriedgISSTLPSKESRRKGGLdylkqvenETRNKseneknrnqednKVKDLNQEIEKLKTQIKHF----ESL 308
Cdd:pfam05483 430 -------------IAEELKGKEQELIFLL--------QAREK------------EIHDLEIQLTAIKTSEEHYlkevEDL 476
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2065208820 309 EEELKKMKSKNNDLQDNYLSEQNKNKLLASQLEEIKLQIKKQKELENGEVEGEDAFL 365
Cdd:pfam05483 477 KTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERML 533
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
19-352 |
5.18e-05 |
|
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: 47.73 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 19 KLQSLSRRLDELEEATKNLQKAEDELLDLQDKV-IQAEGSNSSMLAEIEVLRQRVLRIE--------GKDEEIKRAEDLC 89
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLLNQEKTELLVEQGRLqLQADRHQEHIRARDSLIQSLATRLEldgfergpFSERQIKNFHTLV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 90 RLMKEKLEEEEN-LTRELKSEIERLQKRMAELEKLEEAFSRSKNdctqlclslNEERNLTKKISsELEMLRVKVKELESS 168
Cdd:TIGR00606 400 IERQEDEAKTAAqLCADLQSKERLKQEQADEIRDEKKGLGRTIE---------LKKEILEKKQE-ELKFVIKELQQLEGS 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 169 EDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEK--LIKELTQKLEQNKKMNRDYT--RNASNLERNDLRIED 244
Cdd:TIGR00606 470 SDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKadLDRKLRKLDQEMEQLNHHTTtrTQMEMLTKDKMDKDE 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 245 GISSTLPSKESRRKGGLDYL--KQVENETRNKSENEKNRNQEDnkVKDLNQEIEKLKTQIKHFeslEEELKKMKSKNNDL 322
Cdd:TIGR00606 550 QIRKIKSRHSDELTSLLGYFpnKKQLEDWLHSKSKEINQTRDR--LAKLNKELASLEQNKNHI---NNELESKEEQLSSY 624
|
330 340 350
....*....|....*....|....*....|
gi 2065208820 323 QDNyLSEQNKNKLLASQLEEIKLQIKKQKE 352
Cdd:TIGR00606 625 EDK-LFDVCGSQDEESDLERLKEEIEKSSK 653
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
10-349 |
5.36e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 10 TASSRHLRFKLQSLSRRLDELEEATKNLQKAEDELLDLQDKVIQAEgsnssmlAEIEVLRQrvlRIEGKDEEIKRAEDLC 89
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR-------SELEQLEE---ELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 90 RLMKEKLEEEENLTRELKSEIERLQKrmaELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKELESSE 169
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQK---ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 170 DRLDKTEqsLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLRIEDGISST 249
Cdd:COG4372 174 QALSEAE--AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 250 LPSKESRRKGGLDYLKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMKSKNNDLQDNYLSE 329
Cdd:COG4372 252 LEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELA 331
|
330 340
....*....|....*....|
gi 2065208820 330 QNKNKLLASQLEEIKLQIKK 349
Cdd:COG4372 332 LAILLAELADLLQLLLVGLL 351
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
19-214 |
7.17e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 19 KLQSLSRRLDELEEATKNLQKAEDELLD-LQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEIKRAEDLCRLMKEKLE 97
Cdd:PRK03918 550 KLEELKKKLAELEKKLDELEEELAELLKeLEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELD 629
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 98 EEENLTRELKSEIERLQKRMAELEKL--EEAFSRSkndctqlclslneeRNLTKKISSELEMLRVKVKELESSEDRLDKT 175
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEKKysEEEYEEL--------------REEYLELSRELAGLRAELEELEKRREEIKKT 695
|
170 180 190
....*....|....*....|....*....|....*....
gi 2065208820 176 EQSLASELEKLKsltlsfvserkylnEKEKENEKLIKEL 214
Cdd:PRK03918 696 LEKLKEELEERE--------------KAKKELEKLEKAL 720
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
78-359 |
7.45e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 78 KDEEIKRAEDLCRLMKEKLEEEENLTRELKSEIERlqKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSEL-- 155
Cdd:PTZ00121 1511 KADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK--KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAkk 1588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 156 -EMLRVKVKELESSEDRLDKTEQSLASELEKLKSLTLsfvserkylnEKEKENEKLIKELTQKLEQNKKMNRDYTRNAsn 234
Cdd:PTZ00121 1589 aEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL----------KKAEEEKKKVEQLKKKEAEEKKKAEELKKAE-- 1656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 235 lERNDLRIEDgisstLPSKESRRKGGLDYLKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKTQikhfeslEEELKK 314
Cdd:PTZ00121 1657 -EENKIKAAE-----EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKK-------AEELKK 1723
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2065208820 315 MKSKNNDLQDNYLSEQNKNKLLASQL---EEIKLQIKKQKELENGEVE 359
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEEDKKKAEEAkkdEEEKKKIAHLKKEEEKKAE 1771
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
16-354 |
7.64e-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: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 16 LRFKLQSLSRRLDELEEATKNLQKaedelldLQDKviqaegsNSSMLAEIEVLRQRVLRIEGKDEEIKRAEDlcrlmkek 95
Cdd:pfam01576 157 LEERISEFTSNLAEEEEKAKSLSK-------LKNK-------HEAMISDLEERLKKEEKGRQELEKAKRKLE-------- 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 96 leeeeNLTRELKSEIERLQKRMAEL--------EKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEML------RVK 161
Cdd:pfam01576 215 -----GESTDLQEQIAELQAQIAELraqlakkeEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLeseraaRNK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 162 V--------KELES----SEDRLDKT--EQSLAS----ELEKLK-SLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNK 222
Cdd:pfam01576 290 AekqrrdlgEELEAlkteLEDTLDTTaaQQELRSkreqEVTELKkALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAK 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 223 --KMNRDYTRNASNLERNDLRIEDGISSTLPSKESRRKGGLDylKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKT 300
Cdd:pfam01576 370 rnKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLE--GQLQELQARLSESERQRAELAEKLSKLQSELESVSS 447
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2065208820 301 QIKHFES----LEEELKKMKSKNNDLQDnYLSEQNKNKLLAS----QLEEIKLQIKKQKELE 354
Cdd:pfam01576 448 LLNEAEGknikLSKDVSSLESQLQDTQE-LLQEETRQKLNLStrlrQLEDERNSLQEQLEEE 508
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
146-506 |
1.18e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 46.58 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 146 NLTKKISSELEMLRVKVKELES-SEDRLD---KTEQSLASELEKLKsltlsFVSERKYlnEKEKENEKLIKELTQKLEQN 221
Cdd:PTZ00108 999 YLLGKLERELARLSNKVRFIKHvINGELVitnAKKKDLVKELKKLG-----YVRFKDI--IKKKSEKITAEEEEGAEEDD 1071
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 222 KKMNRDYTRNASNLERNDLRIEDGISS-TLPSKEsrrkggldYLKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKT 300
Cdd:PTZ00108 1072 EADDEDDEEELGAAVSYDYLLSMPIWSlTKEKVE--------KLNAELEKKEKELEKLKNTTPKDMWLEDLDKFEEALEE 1143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 301 QIKHFESLEEELKKMKSKNNDLQDNylSEQNKNKLLASQLEEiKLQIKKQKELENGEVEGEDAFLSSKGRHERTKFRGHG 380
Cdd:PTZ00108 1144 QEEVEEKEIAKEQRLKSKTKGKASK--LRKPKLKKKEKKKKK-SSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNS 1220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 381 SEASVSKHTARELSPQHKRERLRNREFALNNENYSLSNRQVSSPSFTNRRAAKASHMGVSTDSGTQETKKTEDrfvPGSS 460
Cdd:PTZ00108 1221 SGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPD---GESN 1297
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2065208820 461 QSEGKKSREQPSVLSRYPPAAQEHSKAWKGTSKPGTESGLKGKVEK 506
Cdd:PTZ00108 1298 GGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTARKKKSKTRVKQ 1343
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
29-332 |
1.41e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 29 ELEEATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEIK-RAEDLCRLMKEKLEEEENLTRELK 107
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLEtQLKVLSRSINKIKQNLEQKQKELK 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 108 SEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKELES--SEDRLDKTEQSLASELEK 185
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFelKKENLEKEIDEKNKEIEE 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 186 LKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLRIEDGISSTLPSKESRRKggldYLK 265
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQ----EVK 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 266 QVE---NETRNKSENEKNRNQED-NKVKDLNQEIEK------------LKTQIK---------HFESLEEELKKMKSKNN 320
Cdd:TIGR04523 649 QIKetiKEIRNKWPEIIKKIKESkTKIDDIIELMKDwlkelslhykkyITRMIRikdlpkleeKYKEIEKELKKLDEFSK 728
|
330
....*....|..
gi 2065208820 321 DLqDNYLSEQNK 332
Cdd:TIGR04523 729 EL-ENIIKNFNK 739
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
25-487 |
1.79e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 25 RRLDELEEATKNLQKAEDelldLQDKVIQAEGSNSSMLAEIEVLRQRVlriEGKDEEIKRAEDLCRLMKEKLEEEENLTR 104
Cdd:PTZ00121 1302 KKADEAKKKAEEAKKADE----AKKKAEEAKKKADAAKKKAEEAKKAA---EAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 105 ELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLclslnEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLASELE 184
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA-----DELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEA 1449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 185 KLKSLTLSFVSERKYLNEKEKENEKLIK--ELTQKLEQNKKMNRDYTRNASNLERNDLriEDGISSTLPSKESRRKGglD 262
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAKKKADEAKKAAE--AKKKADEAKKAEEAKKA--D 1525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 263 YLKQVENETRN---KSENEKNRNQEDNKVKDLNQEIEKLKTQIKhfeSLEEELKKMKSKNNDLQDNyLSEQNKNKLLASQ 339
Cdd:PTZ00121 1526 EAKKAEEAKKAdeaKKAEEKKKADELKKAEELKKAEEKKKAEEA---KKAEEDKNMALRKAEEAKK-AEEARIEEVMKLY 1601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 340 LEEIKLQIKKQKELENGEVEGEDAflsSKGRHERTKFRGHGSEASVSKHTARELSPQHKRERLRNREFALNNENYSLSNR 419
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEEL---KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE 1678
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065208820 420 QVSSPSFTNRRAAKASHMGVSTDSGTQETKKTEDRFVPGSSQSEGKKSREQPSVLSRYPPAAQEHSKA 487
Cdd:PTZ00121 1679 EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
70-357 |
1.92e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.84 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 70 QRVLRIEGKDEEIKRAEDLCRLMKEKleeeenLTRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLTK 149
Cdd:COG5022 800 QPLLSLLGSRKEYRSYLACIIKLQKT------IKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQS 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 150 KISSELEMLRVKVKELESSE--DRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKE------LTQKLEQN 221
Cdd:COG5022 874 AQRVELAERQLQELKIDVKSisSLKLVNLELESEIIELKKSLSSDLIENLEFKTELIARLKKLLNNidleegPSIEYVKL 953
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 222 KKMNRDYTRNaSNLERNDLRIEDGISStLPSKESRRKGGLDYLKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKTQ 301
Cdd:COG5022 954 PELNKLHEVE-SKLKETSEEYEDLLKK-STILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSA 1031
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065208820 302 IKHFESLEEELKKMKS-----KNNDLQDNYLSEQNKNKLLASQLEEIKLQIKKQKELENGE 357
Cdd:COG5022 1032 SKIISSESTELSILKPlqklkGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENL 1092
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
20-418 |
2.20e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 20 LQSLSRRLDELEEATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEIKRAEDLCRLMKEKLEEE 99
Cdd:PRK01156 175 IDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRY 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 100 ENLTRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLS-LNEERNLTKKISSELEMLRVKVKELESSEDRLDKTE-- 176
Cdd:PRK01156 255 ESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNyINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSvl 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 177 QSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKEltqkLEQNKKMNRDYtrnasnlERNDLRIEDGISSTLPSKEsr 256
Cdd:PRK01156 335 QKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKS----IESLKKKIEEY-------SKNIERMSAFISEILKIQE-- 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 257 rkggldylkqVENETRNKSENEKNRNQED--NKVKDLNQEIEKLktqIKHFESLEEELKKMKSKN--------------N 320
Cdd:PRK01156 402 ----------IDPDAIKKELNEINVKLQDisSKVSSLNQRIRAL---RENLDELSRNMEMLNGQSvcpvcgttlgeeksN 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 321 DLQDNY-------LSEQNKNKLLASQLEEIKLQIKKQKE-LENGEVE---GEDAFLSSKgRHERTKFRGHGSEASVSKHT 389
Cdd:PRK01156 469 HIINHYnekksrlEEKIREIEIEVKDIDEKIVDLKKRKEyLESEEINksiNEYNKIESA-RADLEDIKIKINELKDKHDK 547
|
410 420 430
....*....|....*....|....*....|..
gi 2065208820 390 ARELSPQHKR---ERLRNREFALNNENYSLSN 418
Cdd:PRK01156 548 YEEIKNRYKSlklEDLDSKRTSWLNALAVISL 579
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
8-188 |
2.47e-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: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 8 KETASSRHLRFKLQSLSRRLDELEEAtknLQKAEDELLDLQDKVIQAEgsnssmlAEIEVLRQRVLRIEGKDEEikraed 87
Cdd:COG4913 278 RAALRLWFAQRRLELLEAELEELRAE---LARLEAELERLEARLDALR-------EELDELEAQIRGNGGDRLE------ 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 88 lcrlmkekleeeenltrELKSEIERLQKRMAELEKLEEAFSRsknDCTQLCLSLNEE-----------RNLTKKISSELE 156
Cdd:COG4913 342 -----------------QLEREIERLERELEERERRRARLEA---LLAALGLPLPASaeefaalraeaAALLEALEEELE 401
|
170 180 190
....*....|....*....|....*....|..
gi 2065208820 157 MLRVKVKELESSEDRLDKTEQSLASELEKLKS 188
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
12-186 |
2.63e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 12 SSRHLRFKLQSLSRRLDELEEATKNLQKAEDelldLQDKVIQAEGSNSSMLAEIEVLRQRVlriegkDEEIKRAEDLCRL 91
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLRQQQNAER----LLEEFCQRIGQQLDAAEELEELLAEL------EAQLEELEEQAAE 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 92 MKEKLeeeenltRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDR 171
Cdd:COG3096 576 AVEQR-------SELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDE 648
|
170
....*....|....*
gi 2065208820 172 LDKTEQSLASELEKL 186
Cdd:COG3096 649 LAARKQALESQIERL 663
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
8-372 |
3.19e-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: 44.96 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 8 KETASSRHLRfKLQslsrrlDELEEATKNLQKAEDELLDLQDKVIQAEgsnsSMLAEIEVLRQRVLRIEGKDEEIKRAED 87
Cdd:TIGR00618 373 QQHTLTQHIH-TLQ------QQKTTLTQKLQSLCKELDILQREQATID----TRTSAFRDLQGQLAHAKKQQELQQRYAE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 88 LCRLMKEKLEEEENLT----RELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVK 163
Cdd:TIGR00618 442 LCAAAITCTAQCEKLEkihlQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDID 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 164 ELESSEDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKElTQKLEQnkKMNRdYTRNASNLERNDLRIE 243
Cdd:TIGR00618 522 NPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS-FSILTQ--CDNR-SKEDIPNLQNITVRLQ 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 244 DGISSTLPSKESRRKGGLDYLKQVENETRN--KSENEKNRNQEDNKVK-DLNQEIEKL-KTQIKHFESLEEELKKMKSKN 319
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQPEQDLqdVRLHLQQCSQELALKLtALHALQLTLtQERVREHALSIRVLPKELLAS 677
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2065208820 320 NDLQDNYlsEQNKNKLLASQLEEIKLQIKKQKELEngEVEGEdaflSSKGRHE 372
Cdd:TIGR00618 678 RQLALQK--MQSEKEQLTYWKEMLAQCQTLLRELE--THIEE----YDREFNE 722
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
76-368 |
3.27e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 76 EGKDEEIKRAEDLCRLMKEKLEEEENLTRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSEL 155
Cdd:COG4372 31 EQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 156 EMLRVKVKELESSEDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKmnRDYTRNASNL 235
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 236 ERNDLRIEDGISSTLPSKESRRKGGLDYLKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKM 315
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2065208820 316 KSKNNDLQDNYLSEQNKNKLLASQLEEIKLQIKKQKELENGEVEGEDAFLSSK 368
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
16-192 |
3.35e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 16 LRFKLQSLSRRLDELE----EATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQR-----VLRIEGKDEEIKRAE 86
Cdd:COG4942 60 LERRIAALARRIRALEqelaALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalLLSPEDFLDAVRRLQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 87 DLcrlmkekleeeENLTRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERN-----------LTKKISSEL 155
Cdd:COG4942 140 YL-----------KYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAalealkaerqkLLARLEKEL 208
|
170 180 190
....*....|....*....|....*....|....*..
gi 2065208820 156 EMLRVKVKELESSEDRLDKTEQSLASELEKLKSLTLS 192
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2-346 |
3.64e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 2 AEFTSYKETASSRHLrfkLQSLSRRLDELEEATKNLQKAEDELLDLQD--KVIQAEGSNssmlaeievlrqrVLRIEGKD 79
Cdd:COG3206 81 SPLETQIEILKSRPV---LERVVDKLNLDEDPLGEEASREAAIERLRKnlTVEPVKGSN-------------VIEISYTS 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 80 EEIKRAEDLC---------RLMKEKLEEEENLTRELKSEIERLQKRMAELEKLEEAFSRSKNDctqlcLSLNEERNLTKK 150
Cdd:COG3206 145 PDPELAAAVAnalaeayleQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGL-----VDLSEEAKLLLQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 151 ISSELEMLRVKVK-ELESSEDRLDKTEQSLASELEklkslTLSFVSERKYLNEKEKEneklIKELTQKLEQnkkMNRDYT 229
Cdd:COG3206 220 QLSELESQLAEARaELAEAEARLAALRAQLGSGPD-----ALPELLQSPVIQQLRAQ----LAELEAELAE---LSARYT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 230 RNASNLERNDLRIEDgisstlpskesrrkggldYLKQVENETRNKSENEKNRNQE-DNKVKDLNQEIEKLKTQIKHFESL 308
Cdd:COG3206 288 PNHPDVIALRAQIAA------------------LRAQLQQEAQRILASLEAELEAlQAREASLQAQLAQLEARLAELPEL 349
|
330 340 350
....*....|....*....|....*....|....*...
gi 2065208820 309 EEELkkmksknNDLQDNYLSEQNKNKLLASQLEEIKLQ 346
Cdd:COG3206 350 EAEL-------RRLEREVEVARELYESLLQRLEEARLA 380
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
28-244 |
4.01e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.09 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 28 DELEEATKNLQKAEDELLDLQDKVIQAEgsnssmlAEIEVLRQRVLRIEgkdEEIKRAEdlcrlmkekleeeenltrelk 107
Cdd:pfam00261 8 EELDEAEERLKEAMKKLEEAEKRAEKAE-------AEVAALNRRIQLLE---EELERTE--------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 108 seiERLQKRMAELEKLEEAFSRSKNDC--------------TQLCLSLNEERNLTKKISSELEMLRVKVK----ELESSE 169
Cdd:pfam00261 57 ---ERLAEALEKLEEAEKAADESERGRkvlenralkdeekmEILEAQLKEAKEIAEEADRKYEEVARKLVvvegDLERAE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 170 DRLDKTE---QSLASEL----EKLKSLTlsfVSERKYlNEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLRI 242
Cdd:pfam00261 134 ERAELAEskiVELEEELkvvgNNLKSLE---ASEEKA-SEREDKYEEQIRFLTEKLKEAETRAEFAERSVQKLEKEVDRL 209
|
..
gi 2065208820 243 ED 244
Cdd:pfam00261 210 ED 211
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
101-349 |
4.42e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.44 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 101 NLTRELKSEIERLQKRM---------AELEKLEEAFSRSK-----NDCTQLcLSLNEERNLTKKISSELEMLRVKVKELE 166
Cdd:PTZ00440 933 NLLNNLNKEKEKIEKQLsdtkinnlkMQIEKTLEYYDKSKeningNDGTHL-EKLDKEKDEWEHFKSEIDKLNVNYNILN 1011
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 167 SSEDRLDKTEQslaselEKLKSLTLSFVSERKY-LNEKEKENEKLIKELTQKLeQNKKMNRDYTRNASNLERNDLRIEDG 245
Cdd:PTZ00440 1012 KKIDDLIKKQH------DDIIELIDKLIKEKGKeIEEKVDQYISLLEKMKTKL-SSFHFNIDIKKYKNPKIKEEIKLLEE 1084
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 246 ISSTLPSKESRRKGGLDYLKQVENETRNKSENEKNRNQE--DNKVKDLNQEIEKLKTQIKHFESLEEELKKMKSKNN--- 320
Cdd:PTZ00440 1085 KVEALLKKIDENKNKLIEIKNKSHEHVVNADKEKNKQTEhyNKKKKSLEKIYKQMEKTLKELENMNLEDITLNEVNEiei 1164
|
250 260 270
....*....|....*....|....*....|....
gi 2065208820 321 ---DLQDNYLSEQ--NKNKLLASQLEEIKLQIKK 349
Cdd:PTZ00440 1165 eyeRILIDHIVEQinNEAKKSKTIMEEIESYKKD 1198
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
15-346 |
4.66e-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: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 15 HLRFKLQSLSRRLDELEE--------------------ATKNLQKAEDELLDLQDKVIQAEgsNSSMLAEIEVLRQRVLR 74
Cdd:TIGR00618 390 TLTQKLQSLCKELDILQReqatidtrtsafrdlqgqlaHAKKQQELQQRYAELCAAAITCT--AQCEKLEKIHLQESAQS 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 75 IEGKDEEIKRAEDLCRLMKEKLEEEENLTRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLTK---KI 151
Cdd:TIGR00618 468 LKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETseeDV 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 152 SSELEMLRVKVKELESSEDRLDKTEQSLASELEKLKSL---TLSFVSERKYLNEKEKENEKLIKELTQKL------EQNK 222
Cdd:TIGR00618 548 YHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDipnLQNITVRLQDLTEKLSEAEDMLACEQHALlrklqpEQDL 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 223 KMNRDYTRNASNLERNDLRIEDGISSTLPSKESR------RKGGLDYLKQVEN---ETRNKSENEKNRNQEDNKVKDLNQ 293
Cdd:TIGR00618 628 QDVRLHLQQCSQELALKLTALHALQLTLTQERVRehalsiRVLPKELLASRQLalqKMQSEKEQLTYWKEMLAQCQTLLR 707
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2065208820 294 EIE-KLKTQIKHFESLEEELKKMKSKNNdlQDNYLSEQNKNKLLASQLEEIKLQ 346
Cdd:TIGR00618 708 ELEtHIEEYDREFNEIENASSSLGSDLA--AREDALNQSLKELMHQARTVLKAR 759
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
25-470 |
4.85e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 25 RRLDELEEATKNLQKAEDELLDLQDKVIQAE--GSNSSMLAEIEVLRQRVLRIEGKDEEIKRAEDLCRLmkekleeeenl 102
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKKAEEERNNEEIRKFEEArmAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKA----------- 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 103 trELKSEIERLQKRMAELEKLEEAFSRSKNdctqlclSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEqslase 182
Cdd:PTZ00121 1299 --EEKKKADEAKKKAEEAKKADEAKKKAEE-------AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE------ 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 183 lEKLKSLTLSFVSERKYLNEKEKENEKLIK--ELTQKLEQNKKMNRDYTRNASNLERND---LRIEDGISSTLPSKESRR 257
Cdd:PTZ00121 1364 -EKAEAAEKKKEEAKKKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAAAAKKKADeakKKAEEKKKADEAKKKAEE 1442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 258 KGGLDYLKQVENETRnKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMKSKNNDLQDNYLSEQNKNKLLA 337
Cdd:PTZ00121 1443 AKKADEAKKKAEEAK-KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 338 SQLEEIKLQIKKQKELENGEVEGEDAFLSSKGRHERTKFRGHGSEASVSKHTARELSPQHKRERLRNREFALNNENYSLS 417
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2065208820 418 NRQVSSPSFTNRRAAKASHMGVSTDSGTQETKKTEDrfvPGSSQSEGKKSREQ 470
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ---LKKKEAEEKKKAEE 1651
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
105-387 |
6.32e-04 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.79 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 105 ELKSEIERLQKRMAELEKLE--EAFSRSKNDCTQLCLSLNE-----------ERNLTKKISSELEMLRVKVKELESSEDR 171
Cdd:COG5185 286 NLIKQFENTKEKIAEYTKSIdiKKATESLEEQLAAAEAEQEleeskretetgIQNLTAEIEQGQESLTENLEAIKEEIEN 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 172 LDKTEQSLASElEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNrdyTRNASNLERN----------DLR 241
Cdd:COG5185 366 IVGEVELSKSS-EELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAA---DRQIEELQRQieqatssneeVSK 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 242 IEDGISSTLpsKESRRKGGLDYLKQVENETRN-KSENEKNRNQEDNKVKDLNQEIEKLKTQI-KHFESLEEELKKMKSKN 319
Cdd:COG5185 442 LLNELISEL--NKVMREADEESQSRLEEAYDEiNRSVRSKKEDLNEELTQIESRVSTLKATLeKLRAKLERQLEGVRSKL 519
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065208820 320 NDLQDNYLSEQNKNKLLASQLEEIKLQIKKQKELENGEVEGEDAFLSSKGRHERTKFRGHGSEASVSK 387
Cdd:COG5185 520 DQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQYLSTIESQQARE 587
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
16-365 |
8.23e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 8.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 16 LRFKLQSLSRrldELEEATKNLQKAEDELldlqDKVIQAEGSNSSMLAEIEVLRQrvLRIEGKDEEIKRAE--------D 87
Cdd:TIGR00606 749 LRNKLQKVNR---DIQRLKNDIEEQETLL----GTIMPEEESAKVCLTDVTIMER--FQMELKDVERKIAQqaaklqgsD 819
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 88 LCRLMKEKLEEEENLTRELK---SEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKE 164
Cdd:TIGR00606 820 LDRTVQQVNQEKQEKQHELDtvvSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQS 899
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 165 LESSEDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLRIE- 243
Cdd:TIGR00606 900 LIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETEl 979
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 244 DGISSTLPSKESRRkggldylKQVENETRNKSENEKNRNQEDNKVKD------LNQEIEKLKTQIKHF--ESLEEELKKM 315
Cdd:TIGR00606 980 NTVNAQLEECEKHQ-------EKINEDMRLMRQDIDTQKIQERWLQDnltlrkRENELKEVEEELKQHlkEMGQMQVLQM 1052
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2065208820 316 KSKNNDLQDNYLSEQNKNKLLASQLEEIKLQIK------KQKELENGEVEGEDAFL 365
Cdd:TIGR00606 1053 KQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKhfkkelREPQFRDAEEKYREMMI 1108
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
149-226 |
8.47e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 149 KKISSELEM-LRVKVKELESSEDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKL-EQNKKMNR 226
Cdd:PRK12704 67 HKLRNEFEKeLRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIeEQLQELER 146
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
14-351 |
9.91e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 9.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 14 RHLRFKLQSLSRRLDELEEATKNLQKAEDELLDLQDKVIQAEgsnssmlAEIEVLRQRVlriegKDEEIKRAEDLCRLMK 93
Cdd:COG4717 135 EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQ-------EELEELLEQL-----SLATEEELQDLAEELE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 94 EKLEEEENLTRELKSEIERLQKRMAELEKLEEAfSRSKNDCTQLclslnEERNLTKKISSELEMLRVKVKELESSEDRL- 172
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENE-LEAAALEERL-----KEARLLLLIAAALLALLGLGGSLLSLILTIa 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 173 --------------------------DKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENE-----KLIKELTQKLEQN 221
Cdd:COG4717 277 gvlflvlgllallflllarekaslgkEAEELQALPALEELEEEELEELLAALGLPPDLSPEEllellDRIEELQELLREA 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 222 KKMNRDYTRNASNLERNDLRIEDGISS--------------------------TLPSKESRRKGGLDYLKQVENETRnKS 275
Cdd:COG4717 357 EELEEELQLEELEQEIAALLAEAGVEDeeelraaleqaeeyqelkeeleeleeQLEELLGELEELLEALDEEELEEE-LE 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 276 ENEKNRNQEDNKVKDLNQEIEKLKTQIKHFES------LEEELKKMKSKNNDLQDNYLSeqnkNKLLASQLEEIKLQIKK 349
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEdgelaeLLQELEELKAELRELAEEWAA----LKLALELLEEAREEYRE 511
|
..
gi 2065208820 350 QK 351
Cdd:COG4717 512 ER 513
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
27-359 |
1.06e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.28 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 27 LDELEEATKNLQKAEDELLDLQDKVIQAEGSNSS--MLAEIEVLRQRvlrIEGKDEEIKRAEDLcrlmkekleeeenltr 104
Cdd:PTZ00440 690 IKNLKKELQNLLSLKENIIKKQLNNIEQDISNSLnqYTIKYNDLKSS---IEEYKEEEEKLEVY---------------- 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 105 eLKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVK----ELESSEDRLDKTEQSLA 180
Cdd:PTZ00440 751 -KHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILNKENKISNDINILKENKKnnqdLLNSYNILIQKLEAHTE 829
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 181 SELEKLKSLTLSFVSERKYLNEKEKENEklIKELTQKLEQNKKMNRDYTRNASNLERNDLRIeDGISSTLPSKES--RRK 258
Cdd:PTZ00440 830 KNDEELKQLLQKFPTEDENLNLKELEKE--FNENNQIVDNIIKDIENMNKNINIIKTLNIAI-NRSNSNKQLVEHllNNK 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 259 GGL-----DYLKQVENET-------------RNKSENEKNRNQEDNKVKDLNQEIEKL---------------KTQIKHF 305
Cdd:PTZ00440 907 IDLknkleQHMKIINTDNiiqkneklnllnnLNKEKEKIEKQLSDTKINNLKMQIEKTleyydkskeningndGTHLEKL 986
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2065208820 306 ESLEEELKKMKSKNNDLQDNY-LSEQNKNKLLASQLEEIKLQIKKQKELENGEVE 359
Cdd:PTZ00440 987 DKEKDEWEHFKSEIDKLNVNYnILNKKIDDLIKKQHDDIIELIDKLIKEKGKEIE 1041
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
110-385 |
1.21e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 110 IERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLASELEKLKSL 189
Cdd:pfam12128 233 IAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 190 TLSFVSERKYlnEKEKENEKLIKELTQKLEQNKKmnrdytrnasnlernDLRIEDGISSTLPSKESRRKGGLDYLKQVEN 269
Cdd:pfam12128 313 ADAAVAKDRS--ELEALEDQHGAFLDADIETAAA---------------DQEQLPSWQSELENLEERLKALTGKHQDVTA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 270 ETRNKSENEKNRNQEDnkVKDLNQEIEKLK-TQIKHFESLEEELKKMKSKNNDLQDNYLSEQNKNKL-LASQLEEIKLQI 347
Cdd:pfam12128 376 KYNRRRSKIKEQNNRD--IAGIKDKLAKIReARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYrLKSRLGELKLRL 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2065208820 348 --------------KKQKELENGEVEGEDAFLS-SKGRHERTKFRGHGSEASV 385
Cdd:pfam12128 454 nqatatpelllqleNFDERIERAREEQEAANAEvERLQSELRQARKRRDQASE 506
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
4-357 |
1.23e-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: 43.11 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 4 FTSYKETASSRHLRFKLQSLSRRLDELEEATKNLQKAEDELLDLQDKVIQAEGSNSSML-------AEIEVLRQRVLRIE 76
Cdd:TIGR00606 179 FSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSReivksyeNELDPLKNRLKEIE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 77 GKDEEIKRAEDLCRLMKEKLEEEENLTRELKSEIERL----QKRMAELEKLEEAFSRSKN----DCTQLCLSLNEERNLT 148
Cdd:TIGR00606 259 HNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVfqgtDEQLNDLYHNHQRTVREKErelvDCQRELEKLNKERRLL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 149 KKISSELEmlrVKVKELESSEDRLDktEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMnrdy 228
Cdd:TIGR00606 339 NQEKTELL---VEQGRLQLQADRHQ--EHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKT---- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 229 trnaSNLERNDLRIEDGISSTLPSKESRRKGGLDYLKQVENETRNKSENEknrnqednkVKDLNQEIEKLKTQIKHFESL 308
Cdd:TIGR00606 410 ----AAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEE---------LKFVIKELQQLEGSSDRILEL 476
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2065208820 309 EEELKKMKSKNNDLQDNYLSEQNKNKLLASQLEEIKLQIKKQKELENGE 357
Cdd:TIGR00606 477 DQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEME 525
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
153-369 |
1.27e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 153 SELEMLRVKVKELESSEDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTRNA 232
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 233 SNLERNDLRIEDGISSTLPSKESRRkggLDYLKQVENetrnkseneknrnQEDNKVKDLNQEIEKLKTQIKHFESLEEEL 312
Cdd:COG3883 96 YRSGGSVSYLDVLLGSESFSDFLDR---LSALSKIAD-------------ADADLLEELKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2065208820 313 KKMKSKNNDLQDNYLSEQNKNKLLASQLEEIKLQIKKQKELENGEVEGEDAFLSSKG 369
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
19-344 |
1.29e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 19 KLQSLSRRLDELEEATKNLQKAEDELLDLQDKVIQaegsNSSMLAEievlrQRVLRIEGKDEEIKRAEDLCRLMKEKLEE 98
Cdd:PRK01156 410 ELNEINVKLQDISSKVSSLNQRIRALRENLDELSR----NMEMLNG-----QSVCPVCGTTLGEEKSNHIINHYNEKKSR 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 99 EENLTRELKSEIERLQKRMAELEKLEEAFSRSKndctqlclsLNEERNLTKKISSelemLRVKVKELESSEDRLDKTEQS 178
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKIVDLKKRKEYLESEE---------INKSINEYNKIES----ARADLEDIKIKINELKDKHDK 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 179 LASELEKLKSLTLSFVSERK--YLNEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNdlrIEDgISSTLPSkesr 256
Cdd:PRK01156 548 YEEIKNRYKSLKLEDLDSKRtsWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIG---FPD-DKSYIDK---- 619
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 257 rkggldYLKQVENETRNkSENEKNRNQEDNKVKD-LNQEIEKLKTQIKHFESLEEELKKMKSKNNDLQDNYlseqnknKL 335
Cdd:PRK01156 620 ------SIREIENEANN-LNNKYNEIQENKILIEkLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNL-------KK 685
|
....*....
gi 2065208820 336 LASQLEEIK 344
Cdd:PRK01156 686 SRKALDDAK 694
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
104-240 |
1.32e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 104 RELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLcLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKteqsLASEL 183
Cdd:COG4913 620 AELEEELAEAEERLEALEAELDALQERREALQRL-AEYSWDEIDVASAEREIAELEAELERLDASSDDLAA----LEEQL 694
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2065208820 184 EKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDL 240
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
113-224 |
1.41e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 113 LQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNltKKISSELEMLRVKVKELESSEDRLDKTEQSLASELEKLKSLTLS 192
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEI--RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR 459
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2065208820 193 FVSERKYLNEKEKENEKL----------IKELTQKLEQNKKM 224
Cdd:COG2433 460 EIRKDREISRLDREIERLereleeererIEELKRKLERLKEL 501
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
254-393 |
1.55e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 41.64 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 254 ESRRKggLDYLKQVENETRNKSENEKNRNQE-DNKVKDLNQEIEKLKTQIKhfeSLEEELKKMKSKNNDLQDNYLSEQNK 332
Cdd:COG4026 132 ELREE--LLELKEKIDEIAKEKEKLTKENEElESELEELREEYKKLREENS---ILEEEFDNIKSEYSDLKSRFEELLKK 206
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2065208820 333 NKLLASQLEEiklqikKQKELENGEVEGEDAFL-SSKGRHERTKFRGHGSEASVSKHTAREL 393
Cdd:COG4026 207 RLLEVFSLEE------LWKELFPEELPEEDFIYfATENLKPGKIIVGQGYIAAESKEDAEEW 262
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
12-220 |
1.69e-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: 41.93 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 12 SSRHLRFKLQSLSRRLDELEEAT--------KNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEIK 83
Cdd:smart00787 71 SCKELKKYISEGRDLFKEIEEETlinnpplfKEYFSASPDVKLLMDKQFQLVKTFARLEAKKMWYEWRMKLLEGLKEGLD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 84 RAEDLCRLMKEKLEEEENLTRELKSEI-ERLQKRMAELEKLEEAfSRSKNDCTQlclslNEERNLTKKISSELEMLRVKV 162
Cdd:smart00787 151 ENLEGLKEDYKLLMKELELLNSIKPKLrDRKDALEEELRQLKQL-EDELEDCDP-----TELDRAKEKLKKLLQEIMIKV 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2065208820 163 KELESSEDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQ 220
Cdd:smart00787 225 KKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKL 282
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
107-359 |
1.70e-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: 42.42 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 107 KSEIERLQKRMAELEKLEEAFSRSKNDCTQLclslNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLASELEKL 186
Cdd:pfam17380 326 QAEMDRQAAIYAEQERMAMERERELERIRQE----ERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 187 KSLTLSFVSERKYLNEKEKENEKLIKEltQKLEQNKKMNRDYTRNASNLERndLRIEdgisstlpskESRRKGGLDYLKQ 266
Cdd:pfam17380 402 RKVKILEEERQRKIQQQKVEMEQIRAE--QEEARQREVRRLEEERAREMER--VRLE----------EQERQQQVERLRQ 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 267 VENEtRNKSENEKNRNQEDnkvkdlNQEIEKLKTQIkhfesLEEELKKMKSKnndlqdnYLSEQNKNKLLASQLEEIKLQ 346
Cdd:pfam17380 468 QEEE-RKRKKLELEKEKRD------RKRAEEQRRKI-----LEKELEERKQA-------MIEEERKRKLLEKEMEERQKA 528
|
250
....*....|...
gi 2065208820 347 IKKQKELENGEVE 359
Cdd:pfam17380 529 IYEEERRREAEEE 541
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
19-362 |
1.76e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.35 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 19 KLQSLSRRLDELEEATKNLQKaedELLDLQDKVIQAEGSNSSmlAEIEvlrQRVLRIEGK--------DEEIKRAEDLCR 90
Cdd:PRK10929 66 RAKQYQQVIDNFPKLSAELRQ---QLNNERDEPRSVPPNMST--DALE---QEILQVSSQlleksrqaQQEQDRAREISD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 91 LMKEKLEEEENLTRELkSEIE-RLQKRMAELEKLEEAfsrskndctQLcLSLNEERNLTKKISSELEM-----------L 158
Cdd:PRK10929 138 SLSQLPQQQTEARRQL-NEIErRLQTLGTPNTPLAQA---------QL-TALQAESAALKALVDELELaqlsannrqelA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 159 RVKVKELESSEDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENekLIKELTQKLEQNKKMNRDYTRNAsnlERN 238
Cdd:PRK10929 207 RLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALESTELLAEQSGD--LPKSIVAQFKINRELSQALNQQA---QRM 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 239 DLriedgisstLPSKESRRKGGLDYLKQVENETRNKSE--------NEKNRNQ-----EDNKVKDLNQEIEKLKTQIKHF 305
Cdd:PRK10929 282 DL---------IASQQRQAASQTLQVRQALNTLREQSQwlgvsnalGEALRAQvarlpEMPKPQQLDTEMAQLRVQRLRY 352
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2065208820 306 ESLEEELKKMKSKNNDLQDNYLSEQnkNKLLASQLeeiklqiKKQKELENGEVEGED 362
Cdd:PRK10929 353 EDLLNKQPQLRQIRQADGQPLTAEQ--NRILDAQL-------RTQRELLNSLLSGGD 400
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
19-230 |
1.95e-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: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 19 KLQSLSRRLDELEEAtknLQKAEDELLDLQDKviqaegsnssmLAEIEVLRQRVLRIEGKDEEIKRAEDLCRLMkeklee 98
Cdd:COG4913 611 KLAALEAELAELEEE---LAEAEERLEALEAE-----------LDALQERREALQRLAEYSWDEIDVASAEREI------ 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 99 eenltRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQlclsLNEERNLTKKISSELEmlrvkvKELESSEDRLDKTeQS 178
Cdd:COG4913 671 -----AELEAELERLDASSDDLAALEEQLEELEAELEE----LEEELDELKGEIGRLE------KELEQAEEELDEL-QD 734
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2065208820 179 LASELEKLKSLTLSFVSERKYLNEKEKENEKLIKE-LTQKLEQ-NKKMNRDYTR 230
Cdd:COG4913 735 RLEAAEDLARLELRALLEERFAAALGDAVERELREnLEERIDAlRARLNRAEEE 788
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-363 |
2.14e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 2 AEFTSYKETASSRHLRFKLQSLSRRLDELEEATKNLQKAEDELLDLQDKVIQAEGSNSSMLAE-----------IEVLR- 69
Cdd:PTZ00121 1111 AEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEdakkaeaarkaEEVRKa 1190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 70 ------QRVLRIEG--KDEEIKRAEDLCRLMKEKLEEEENLTRELKSEIERLQK----RMAELEKLEEAFSRSKNDCTQL 137
Cdd:PTZ00121 1191 eelrkaEDARKAEAarKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKaeeeRNNEEIRKFEEARMAHFARRQA 1270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 138 CLSLNEERnltkkisselemlrvKVKELESSEDRLDKTEQSLASELEKLKSLtlsfvserkylnEKEKENEKLIKELTQK 217
Cdd:PTZ00121 1271 AIKAEEAR---------------KADELKKAEEKKKADEAKKAEEKKKADEA------------KKKAEEAKKADEAKKK 1323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 218 LEQNKKMNRDYTRNASNLERND-LRIEDGISSTLPSKESRRKGGLDYLKQveNETRNKSENEKNRNQEDNKVKDLNQEIE 296
Cdd:PTZ00121 1324 AEEAKKKADAAKKKAEEAKKAAeAAKAEAEAAADEAEAAEEKAEAAEKKK--EEAKKKADAAKKKAEEKKKADEAKKKAE 1401
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2065208820 297 KLKTQIKHFESLEEELKKMKSKNNDLQDNYLSEQNKNKL-LASQLEEIKLQIKKQKELENGEVEGEDA 363
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAeEAKKADEAKKKAEEAKKAEEAKKKAEEA 1469
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
30-189 |
2.43e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 30 LEEAtknLQKAEDELLDLQDKVIQAEGSNSSmlAEIEVLRQRVLRiegKDEEIKRAEDlcrlmkekleeeenLTRELKSE 109
Cdd:COG2433 378 IEEA---LEELIEKELPEEEPEAEREKEHEE--RELTEEEEEIRR---LEEQVERLEA--------------EVEELEAE 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 110 IERLQKRMAELE-KLEEAfsrskndctqlclslNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLASELEKLKS 188
Cdd:COG2433 436 LEEKDERIERLErELSEA---------------RSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
.
gi 2065208820 189 L 189
Cdd:COG2433 501 L 501
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
104-355 |
2.45e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.35 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 104 RELKSEIE-RLQKRM-AELEK-LEEAFSRSKNdctqlclslneERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLA 180
Cdd:TIGR01612 524 NIIGFDIDqNIKAKLyKEIEAgLKESYELAKN-----------WKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEID 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 181 SELEKLKSLTLSFVSERKYLNEKEKENEKLIkELTQKLEQNKKMNRDYTRNASNLERNDLRIEDGISSTLPSKESR-RKG 259
Cdd:TIGR01612 593 DEIIYINKLKLELKEKIKNISDKNEYIKKAI-DLKKIIENNNAYIDELAKISPYQVPEHLKNKDKIYSTIKSELSKiYED 671
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 260 GLDYLKqveNETRN-KSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFE--SLEEELKKMKSKNNDLQDNyLSEQNK---- 332
Cdd:TIGR01612 672 DIDALY---NELSSiVKENAIDNTEDKAKLDDLKSKIDKEYDKIQNMEtaTVELHLSNIENKKNELLDI-IVEIKKhihg 747
|
250 260
....*....|....*....|....*
gi 2065208820 333 --NKLLASQLEEIKlqiKKQKELEN 355
Cdd:TIGR01612 748 eiNKDLNKILEDFK---NKEKELSN 769
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
101-224 |
2.60e-03 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 39.47 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 101 NLTRELKSEIERLQKR-MAELEKLEEAFSrskndctqlclslNEERNLTKKISSE--------LEMLRVKVKELESSEDR 171
Cdd:pfam12474 18 QLKKRYEKELEQLERQqKQQIEKLEQRQT-------------QELRRLPKRIRAEqkkrlkmfRESLKQEKKELKQEVEK 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2065208820 172 LDKTEQSlasELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKM 224
Cdd:pfam12474 85 LPKFQRK---EAKRQRKEELELEQKHEELEFLQAQSEALERELQQLQNEKRKE 134
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
109-364 |
2.68e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 109 EIERLqKRMAELEKLEEAFSRSkNDCTQLCLSLNEERNLTKKISSELEmlRVKVKELESSEDRLDKTEQSLASELEKLks 188
Cdd:PRK05771 32 HIEDL-KEELSNERLRKLRSLL-TKLSEALDKLRSYLPKLNPLREEKK--KVSVKSLEELIKDVEEELEKIEKEIKEL-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 189 ltlsfVSERKYLNEKEKENEKLIKELtQKLE------QNKKMNRDYTRNASNLERNDLRIEDGISSTLPSKESRRKGGLD 262
Cdd:PRK05771 106 -----EEEISELENEIKELEQEIERL-EPWGnfdldlSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYISTDKGYV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 263 YLKQVenetrNKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMKSKNNDLQDNYLSEQNKNKLLASQLEE 342
Cdd:PRK05771 180 YVVVV-----VLKELSDEVEEELKKLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYE 254
|
250 260
....*....|....*....|..
gi 2065208820 343 IKLQIKKQKELENGEVEGEDAF 364
Cdd:PRK05771 255 YLEIELERAEALSKFLKTDKTF 276
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
21-325 |
2.87e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.43 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 21 QSLSRRLDELEEATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEIKRA-EDLCRLMKEKLEEE 99
Cdd:COG4372 59 EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKErQDLEQQRKQLEAQI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 100 ENLTRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLclslnEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSL 179
Cdd:COG4372 139 AELQSEIAEREEELKELEEQLESLQEELAALEQELQAL-----SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLP 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 180 ASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLRIEDGISSTLPSKESRRKG 259
Cdd:COG4372 214 RELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAAL 293
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2065208820 260 GLDYLKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMKSKNNDLQDN 325
Cdd:COG4372 294 ELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELL 359
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
33-220 |
2.96e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 33 ATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEIKRAEDlcrlmkekleeeenltrELKSEIER 112
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID-----------------KLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 113 LQKRMAELEKLEEAFSRS--KNDCTQLCLS-----------LNEERNLTKKISSELEMLrvkvKELESSEDRLDKTEQSL 179
Cdd:COG3883 77 AEAEIEERREELGERARAlyRSGGSVSYLDvllgsesfsdfLDRLSALSKIADADADLL----EELKADKAELEAKKAEL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2065208820 180 ASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQ 220
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
14-375 |
3.05e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 3.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 14 RHLRFKLQSLSRRLDELE----EATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRI-EGKDEEIKRAEDL 88
Cdd:pfam01576 408 KKLEGQLQELQARLSESErqraELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTqELLQEETRQKLNL 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 89 CRLMKEKLEEEENLTRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKELESS 168
Cdd:pfam01576 488 STRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAA 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 169 EDRLDKTEQSLASELEklkSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTR---NASNLERNDLRIEDG 245
Cdd:pfam01576 568 YDKLEKTKNRLQQELD---DLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRaeaEAREKETRALSLARA 644
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 246 ISSTLPSKESRRKGGLDYLKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFES-----------LEEELKK 314
Cdd:pfam01576 645 LEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDelqatedaklrLEVNMQA 724
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2065208820 315 MKSK-NNDLQDNYLSEQNKNKLLASQLEEIKLQI-------------KKQKELENGEVEGE-DAflSSKGRHERTK 375
Cdd:pfam01576 725 LKAQfERDLQARDEQGEEKRRQLVKQVRELEAELederkqraqavaaKKKLELDLKELEAQiDA--ANKGREEAVK 798
|
|
| NIP100 |
COG5244 |
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ... |
145-352 |
3.13e-03 |
|
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 227569 [Multi-domain] Cd Length: 669 Bit Score: 41.59 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 145 RNLTKKISSELEMLRvKVKElESSEDRLdKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKM 224
Cdd:COG5244 82 KGGLVCESKGMDKDG-EIKQ-ENHEDRI-HFEESKIRRLEETIEALKSTEKEEIVELRRENEELDKINLSLRERISSEEP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 225 NRD-------YTRNASNLERNDLRIEDGISSTLPSKESRRKGGlDYLKQVENETRNKSENEKNRNQE---DNKVKDLNQE 294
Cdd:COG5244 159 ELNkdgsklsYDELKEFVEESRVQVYDMVELVSDISETLNRNG-SIQRSSVRECERSNIHDVLFLVNgilDGVIDELNGE 237
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065208820 295 IEKLKTQIKHFesleeelkkMKSKNNDLQDNYLSEQNKNKLLASQLE-----EIKLQIKKQKE 352
Cdd:COG5244 238 LERLRRQLVSL---------MSSHGIEVEENSRLKATLEKFQSLELKvntlqEELYQNKLLKK 291
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
26-316 |
3.65e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 26 RLDELEEatKNLQKAEDELLDLQDKVIQAEGSN----SSMLAEIEVLRQRVLRiegkdeeiKRAEDLCRLMKEKLEEEEN 101
Cdd:COG4717 2 KIKELEI--YGFGKFRDRTIEFSPGLNVIYGPNeagkSTLLAFIRAMLLERLE--------KEADELFKPQGRKPELNLK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 102 LTRELKSEIERLQKRMAELEKLEEAfsrskndctqlclsLNEERNLTKKISSELEMLRVKVKELESSED------RLDKT 175
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQEE--------------LEELEEELEELEAELEELREELEKLEKLLQllplyqELEAL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 176 EQSLASELEKLKSLtlsfvsERKYLNEKEKENEklIKELTQKLEQNKKMNRDYTRNASNLERNDLRiedgisstlpskes 255
Cdd:COG4717 138 EAELAELPERLEEL------EERLEELRELEEE--LEELEAELAELQEELEELLEQLSLATEEELQ-------------- 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065208820 256 rrkgglDYLKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFEsLEEELKKMK 316
Cdd:COG4717 196 ------DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA-LEERLKEAR 249
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
106-347 |
4.34e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 106 LKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLASELEK 185
Cdd:PRK01156 171 LKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDM 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 186 LKSLTLSFVSERKYLNEKEKENEKL--IKELTQKLEQNKKM-NRDYTRNASNLeRNDLRIEDGISSTLPSKESRRKGGLD 262
Cdd:PRK01156 251 KNRYESEIKTAESDLSMELEKNNYYkeLEERHMKIINDPVYkNRNYINDYFKY-KNDIENKKQILSNIDAEINKYHAIIK 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 263 YLKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESL----EEELKKMKSKNNDLQDNYLSEQNKNKLLAS 338
Cdd:PRK01156 330 KLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLkkkiEEYSKNIERMSAFISEILKIQEIDPDAIKK 409
|
....*....
gi 2065208820 339 QLEEIKLQI 347
Cdd:PRK01156 410 ELNEINVKL 418
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
27-350 |
4.65e-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: 40.99 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 27 LDELEEATK--NLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQrvlrIEGKD-EEIKRAEDLCRlmkekleeeeNLT 103
Cdd:pfam06160 69 LFEAEELNDkyRFKKAKKALDEIEELLDDIEEDIKQILEELDELLE----SEEKNrEEVEELKDKYR----------ELR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 104 RELKSE-------IERLQKRMAELEKLEEAFSrskndctqlclSLNEE------RNLTKKISSELEMLRVKVKELEsseD 170
Cdd:pfam06160 135 KTLLANrfsygpaIDELEKQLAEIEEEFSQFE-----------ELTESgdyleaREVLEKLEEETDALEELMEDIP---P 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 171 RLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEklIKELTQKLEQNKKM--NRDYTRNASNLERNDLRIeDGISS 248
Cdd:pfam06160 201 LYEELKTELPDQLEELKEGYREMEEEGYALEHLNVDKE--IQQLEEQLEENLALleNLELDEAEEALEEIEERI-DQLYD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 249 TL-------PSKESRRKGGLDYLKQVENETRNK-------------SENEKNRNQE--------DNKVKDLNQEI----- 295
Cdd:pfam06160 278 LLekevdakKYVEKNLPEIEDYLEHAEEQNKELkeelervqqsytlNENELERVRGlekqleelEKRYDEIVERLeekev 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2065208820 296 ------EKLKTQIKHFESLEEELKKMKSKNNDLQDNYLSEQNKNKLLASQLEEIKLQIKKQ 350
Cdd:pfam06160 358 ayselqEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKS 418
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
42-340 |
5.09e-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: 40.65 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 42 DELLDLQDKVIQAEGSNSSML----AEI------EVLRQRVLRIEGKDEEIKRAEDLCRLMKEKLEEEENLTRELKSEIE 111
Cdd:pfam07888 4 DELVTLEEESHGEEGGTDMLLvvprAELlqnrleECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 112 RLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLtkkISSELEMLRVKVKELESSEDRLDKTEQSLASELEKLKSLTL 191
Cdd:pfam07888 84 ELKEELRQSREKHEELEEKYKELSASSEELSEEKDA---LLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 192 SFVSERKylnEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERND---LRIEDGISStlpskesrrkggldyLKQVE 268
Cdd:pfam07888 161 KAGAQRK---EEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDtqvLQLQDTITT---------------LTQKL 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2065208820 269 NET-RNKSENEKNRnqednkvKDLNQEIEKLKTQIKHFESLEEELKKMKSknndLQDNYLSEQNKNKLLASQL 340
Cdd:pfam07888 223 TTAhRKEAENEALL-------EELRSLQERLNASERKVEGLGEELSSMAA----QRDRTQAELHQARLQAAQL 284
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
16-361 |
5.13e-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: 40.87 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 16 LRFKLQSLSRRLDELEEATKNLQKAEDELLD-LQDKVIQAEGSNS---SML----AEIEVLRQRVLRIEGKDEEIKRA-E 86
Cdd:pfam15921 115 LQTKLQEMQMERDAMADIRRRESQSQEDLRNqLQNTVHELEAAKClkeDMLedsnTQIEQLRKMMLSHEGVLQEIRSIlV 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 87 DLCRLMKEKLEEEENLT---------------RELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEER------ 145
Cdd:pfam15921 195 DFEEASGKKIYEHDSMStmhfrslgsaiskilRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRieqlis 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 146 -------NLTKK----------ISSELEMLRVKVK-----------ELESS---------------EDRLDKTEQSLA-- 180
Cdd:pfam15921 275 eheveitGLTEKassarsqansIQSQLEIIQEQARnqnsmymrqlsDLESTvsqlrselreakrmyEDKIEELEKQLVla 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 181 -SELEKLKSLTLSFVSERKYLNEKEK----ENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLRIEDgisstlPSKES 255
Cdd:pfam15921 355 nSELTEARTERDQFSQESGNLDDQLQkllaDLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDD------RNMEV 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 256 RRKGGLdyLKQVENETRNKSENE----KNRNQEDNKVKDLNQEIEKLKTQI-KHFESLEEELKKMKSKNNDLQDNYLSEQ 330
Cdd:pfam15921 429 QRLEAL--LKAMKSECQGQMERQmaaiQGKNESLEKVSSLTAQLESTKEMLrKVVEELTAKKMTLESSERTVSDLTASLQ 506
|
410 420 430
....*....|....*....|....*....|....*
gi 2065208820 331 NKNKLLASQLEEI-KLQIK---KQKELENGEVEGE 361
Cdd:pfam15921 507 EKERAIEATNAEItKLRSRvdlKLQELQHLKNEGD 541
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
152-420 |
5.46e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.83 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 152 SSELEMLRVKVKELES---SEDRLDKTEQSLASE----LEKLKSLTLSFVSERKYLNEKEKENEKLI---KELTQKLEQN 221
Cdd:COG5022 1196 SSEVNDLKNELIALFSkifSGWPRGDKLKKLISEgwvpTEYSTSLKGFNNLNKKFDTPASMSNEKLLsllNSIDNLLSSY 1275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 222 KKMNRDYTRNASNLERNdlrIEDGISSTLPSKESRRKGgldylkqvenetrnKSENEKNRNQEDNKVKDLNQEIEKLKTQ 301
Cdd:COG5022 1276 KLEEEVLPATINSLLQY---INVGLFNALRTKASSLRW--------------KSATEVNYNSEELDDWCREFEISDVDEE 1338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 302 ikhFESLEEELKKMKSKNNDLqdNYLSE--QNKNKLLASQLEEIKLQIK---KQKELEN-------GEVEGEDAFLSSKG 369
Cdd:COG5022 1339 ---LEELIQAVKVLQLLKDDL--NKLDEllDACYSLNPAEIQNLKSRYDpadKENNLPKeilkkieALLIKQELQLSLEG 1413
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2065208820 370 rHERTKfrGHGSEASVSKHTARELSPQH--KRERLRNREFALNNENYSLSNRQ 420
Cdd:COG5022 1414 -KDETE--VHLSEIFSEEKSLISLDRNSiyKEEVLSSLSALLTKEKIALLDRK 1463
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
16-354 |
5.64e-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: 40.86 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 16 LRFKLQSLSRRLDELEEATKNLQKAEDELLDL----QDKVIQAEgSNSSMLAEIEVLRQRVLRIEGKDEEIKRAE-DLCR 90
Cdd:pfam05483 365 LRTEQQRLEKNEDQLKIITMELQKKSSELEEMtkfkNNKEVELE-ELKKILAEDEKLLDEKKQFEKIAEELKGKEqELIF 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 91 LMKEKLEEEENLTRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLN----EERNLTKKISS---ELEMLRVKVK 163
Cdd:pfam05483 444 LLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDklllENKELTQEASDmtlELKKHQEDII 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 164 ELESSEDR-------LDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTrnasnle 236
Cdd:pfam05483 524 NCKKQEERmlkqienLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC------- 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 237 rNDLRiedgisstlpskesrrkggldylKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKTQIKhfeSLEEELKKMK 316
Cdd:pfam05483 597 -NNLK-----------------------KQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVN---KLELELASAK 649
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2065208820 317 SKNNDLQDNYLSEQNKNKL----LASQLEEIKL----QIKKQKELE 354
Cdd:pfam05483 650 QKFEEIIDNYQKEIEDKKIseekLLEEVEKAKAiadeAVKLQKEID 695
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
147-354 |
6.15e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 147 LTKKISSELEML-RVKVKELESSEDRLDKTEQSLASELEKLKSLTlSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMN 225
Cdd:COG4717 47 LLERLEKEADELfKPQGRKPELNLKELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 226 RDYTRNAsnlERNDLRIEdgisstLPSKESRrkggLDYLKQVENETRNKSENEKNRNQEdnkVKDLNQEIEKLKTQI--- 302
Cdd:COG4717 126 QLLPLYQ---ELEALEAE------LAELPER----LEELEERLEELRELEEELEELEAE---LAELQEELEELLEQLsla 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2065208820 303 --KHFESLEEELKKMKSKNNDLQDNYLSEQNKNKLLASQLEEIKLQIKKQKELE 354
Cdd:COG4717 190 teEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
21-256 |
6.83e-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: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 21 QSLSRRLDELEEATKNLQKAED------ELLDLQDKVIQAEGSnssmLAEIEVLRQ--RVLRIEGKDEEIKRAEDLCRLM 92
Cdd:COG4913 228 DALVEHFDDLERAHEALEDAREqiellePIRELAERYAAARER----LAELEYLRAalRLWFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 93 KekleeeenltRELKSEIERLQKRMAELEKLEEAFSRSKNDctqlcLSLNEERNLTKkissELEMLRVKVKELESSEDRL 172
Cdd:COG4913 304 L----------ARLEAELERLEARLDALREELDELEAQIRG-----NGGDRLEQLER----EIERLERELEERERRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 173 DK-----------TEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLR 241
Cdd:COG4913 365 EAllaalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA 444
|
250
....*....|....*
gi 2065208820 242 IEDGISSTLPSKESR 256
Cdd:COG4913 445 LRDALAEALGLDEAE 459
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
19-475 |
6.90e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.81 E-value: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 19 KLQSLSRRLDELEEATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQrvLRIEGKDEEIKRAEDLCRLMKEKLEE 98
Cdd:TIGR01612 1174 KIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGK--LFLEKIDEEKKKSEHMIKAMEAYIED 1251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 99 EENL---TRELKSEIERLQKRMAELEKLEEAFSRSKNDCTqlcLSLNEERNLTKKISSELEMLRVKVKEleSSEDRLDKT 175
Cdd:TIGR01612 1252 LDEIkekSPEIENEMGIEMDIKAEMETFNISHDDDKDHHI---ISKKHDENISDIREKSLKIIEDFSEE--SDINDIKKE 1326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 176 EQSLASELEKLKSLTLSFVSERKYLNEKEKEN--EKLI---KELTQKLEQNKKMNRDYTRNASNLER---NDLRIED--- 244
Cdd:TIGR01612 1327 LQKNLLDAQKHNSDINLYLNEIANIYNILKLNkiKKIIdevKEYTKEIEENNKNIKDELDKSEKLIKkikDDINLEEcks 1406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 245 GISSTLPSKE----------------SRRKGGLDYLKQVENETRNKSENEKN------------RNQEDNKVKDLNQEIE 296
Cdd:TIGR01612 1407 KIESTLDDKDidecikkikelknhilSEESNIDTYFKNADENNENVLLLFKNiemadnksqhilKIKKDNATNDHDFNIN 1486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 297 KLKTQIKHFESLEEEL---KKMKSKNNDLQDNYLSEQNK--NKLLASQLEEIKLQIKKQKELENGEVegedaflssKGRH 371
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEAdknAKAIEKNKELFEQYKKDVTEllNKYSALAIKNKFAKTKKDSEIIIKEI---------KDAH 1557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 372 ERTKFRGHGSEASVSKhtarelspqHKRERLRNREFALNNE--NYSLSNRQVSSPSFTNrRAAKASHMGVSTDSGTQETK 449
Cdd:TIGR01612 1558 KKFILEAEKSEQKIKE---------IKKEKFRIEDDAAKNDksNKAAIDIQLSLENFEN-KFLKISDIKKKINDCLKETE 1627
|
490 500
....*....|....*....|....*.
gi 2065208820 450 KTEDRFVPGSSQSEGKKSREQPSVLS 475
Cdd:TIGR01612 1628 SIEKKISSFSIDSQDTELKENGDNLN 1653
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
8-125 |
8.18e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 8.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 8 KETASSRHLRFKLQSLSRRLDELEEATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEIKRAED 87
Cdd:COG1196 666 SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEE 745
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2065208820 88 LCRLMKEKLEEEENLTRE-LKSEIERLQKRMAELEK-----LEE 125
Cdd:COG1196 746 ELLEEEALEELPEPPDLEeLERELERLEREIEALGPvnllaIEE 789
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
106-322 |
9.03e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.00 E-value: 9.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 106 LKSEIERLQKRMAELEKLeeafsrSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDrldkteqSLASELEK 185
Cdd:PHA02562 193 IQQQIKTYNKNIEEQRKK------NGENIARKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIE-------DPSAALNK 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2065208820 186 LKSLTLSFVSERKYLNEKEKENEK--LIKELTQKLEQNKKMNRDYTRNASNLERNDLRIEDGISstlpsKESRRKGGLDY 263
Cdd:PHA02562 260 LNTAAAKIKSKIEQFQKVIKMYEKggVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAID-----ELEEIMDEFNE 334
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2065208820 264 LKQVENETRNKSENEKNRNQ-EDNKVKDLNQEIEKLKTQIKHFES----LEEELKKMKSKNNDL 322
Cdd:PHA02562 335 QSKKLLELKNKISTNKQSLItLVDKAKKVKAAIEELQAEFVDNAEelakLQDELDKIVKTKSEL 398
|
|
| |
