|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
52-526 |
6.37e-82 |
|
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.
Pssm-ID: 462869 [Multi-domain] Cd Length: 303 Bit Score: 259.63 E-value: 6.37e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 52 MKELERQQKEIyqvqkkyygldtkwgdieqwmedserysrrfrrntsaSDEDERLSVGSRGSLRAQPeleygspyawtng 131
Cdd:pfam09738 20 MRELERQQKEV-------------------------------------EENADRVFDMSSSSGADTA------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 132 ydgdycgsqslsrrsgrasmldesslygarrgsacgsrapseygshlnsssrassrassaraspvveerpdkdfaeKGSR 211
Cdd:pfam09738 50 ----------------------------------------------------------------------------SGSP 53
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 212 NMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLEL 291
Cdd:pfam09738 54 TASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEM 133
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 292 EEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEeirqlqqkqagfireisdlqetiewkdkkigal 371
Cdd:pfam09738 134 EESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIE--------------------------------- 180
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 372 erqkeffdsirserddlreetvklkeelkKHGIILNSEIATNGEtsdTVNDVGYQAPTKITKEELNALKSAGEGTLDVRL 451
Cdd:pfam09738 181 -----------------------------KHGLVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRL 228
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039727780 452 KKLIDERECLLEQIKKLKGQLEGRQ--KNNKLDLLRAEDGILENGTdaHVMDLQRDANRQISDLKFKLAKSEQEITA 526
Cdd:pfam09738 229 KKLADEKEELLDEVRKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
220-576 |
1.12e-08 |
|
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: 58.53 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 220 TLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQ 299
Cdd:TIGR02168 653 DLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 300 RQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQagfIREISDLQETIewkdkkigalERQKEFFD 379
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA---EAEIEELEAQI----------EQLKEELK 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 380 SIRSERDDLREETVKLKEELKKHGIILNSEIATNGETSDTVNDVGYQAptKITKEELNALKSAGEgTLDVRLKKLIDERE 459
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIE-ELEELIEELESELE 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 460 CLLEQIKKLKGQLEGRQKNnkLDLLRAEdgilENGTDAHVMDLQRDANRqisdLKFKLAKSEQEITALEQNVIRLESQVT 539
Cdd:TIGR02168 877 ALLNERASLEEALALLRSE--LEELSEE----LRELESKRSELRRELEE----LREKLAQLELRLEGLEVRIDNLQERLS 946
|
330 340 350
....*....|....*....|....*....|....*...
gi 1039727780 540 -RYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 576
Cdd:TIGR02168 947 eEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
270-577 |
6.81e-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: 55.84 E-value: 6.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 270 LDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAG 349
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 350 firEISDLQETIEWKDKKIGALERQ--KEFFDSIRSERDDLREETVKLKEELKKHGIILNSEIATNGETSDTVND-VGYQ 426
Cdd:TIGR02169 766 ---RIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElQEQR 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 427 APTKITKEELNALKSAGEGTLDvRLKKLIDERECLLEQIKKLKGQLEGRQKNNKLDLLRAEDGILENGTDAHvmdlqrDA 506
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE------KK 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 507 NRQISDLKFKLAKSEQEITALEQNVIRLES---QVTRYRSAAENAEKIE------------------------DELKAEK 559
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEipeEELSLEDVQAELQRVEeeiralepvnmlaiqeyeevlkrlDELKEKR 995
|
330
....*....|....*...
gi 1039727780 560 RKLQRELRSALDKTEELE 577
Cdd:TIGR02169 996 AKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
324-600 |
2.30e-07 |
|
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: 53.91 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 324 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQkefFDSIRSERDDLREETVKLKEELKKhg 403
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER---IAQLSKELTELEAEIEELEERLEE-- 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 404 iiLNSEIATNGETSDTVNDV--GYQAPTKITKEELNALKSAgEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQKNNKl 481
Cdd:TIGR02168 773 --AEEELAEAEAEIEELEAQieQLKEELKALREALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE- 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 482 dllRAEDGILEngtdahvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRK 561
Cdd:TIGR02168 849 ---ELSEDIES-------------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270
....*....|....*....|....*....|....*....
gi 1039727780 562 LQRELrsaldktEELEVSNGHLVKRLEKMKANRSALLSQ 600
Cdd:TIGR02168 913 LRREL-------EELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
304-600 |
1.20e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 304 EKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKeffDSIRS 383
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL---KELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 384 ERDDLREETVKLKEELkkhgiilnseiatngetsdtvndvgyqaptkitkEELNALKSagegtlDVRLKKLIDERECLLE 463
Cdd:TIGR02169 766 RIEELEEDLHKLEEAL----------------------------------NDLEARLS------HSRIPEIQAELSKLEE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 464 QIKKLKGQL-EGRQKNNKLDLLRAedgILEngtdahvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYR 542
Cdd:TIGR02169 806 EVSRIEARLrEIEQKLNRLTLEKE---YLE--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039727780 543 SAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQ 600
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
299-577 |
2.63e-06 |
|
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: 50.83 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 299 QRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----RQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQ 374
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 375 KEFFDSIR----SERDDLREETVKLKEELkkhgiilnseiatngeTSDTVNDVGYQAPTKITKEELNALKSAgEGTLDVR 450
Cdd:TIGR02168 318 LEELEAQLeeleSKLDELAEELAELEEKL----------------EELKEELESLEAELEELEAELEELESR-LEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 451 LKKLIDERECLLEQIKKLKGQLEgRQKNNKLDLLRAEDGILENGTDAhvmdLQRDANRQISDLKFKLAKSEQEITALEQN 530
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIE-RLEARLERLEDRRERLQQEIEEL----LKKLEEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1039727780 531 VIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELE 577
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
324-598 |
2.84e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 324 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWK-------DKKIGALERQK--------EFFDSIRSER-DD 387
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVkselkelEARIEELEEDLhkleealnDLEARLSHSRiPE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 388 LREETVKLKEELKKHGIILNSeiaTNGETSDTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKK 467
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLRE---IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 468 LKG---QLEGRQKN--NKLDLLRAEDGILENGTDAHVMDLQRdANRQISDLKFKLAKSEQEITALEQNVIRLESQVTryr 542
Cdd:TIGR02169 873 LEAalrDLESRLGDlkKERDELEAQLRELERKIEELEAQIEK-KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE--- 948
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039727780 543 saaenAEKIEDELKAEKRKLQRELRS-------ALDKTEELEVSNGHLVKRLEKMKANRSALL 598
Cdd:TIGR02169 949 -----EELSLEDVQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
328-581 |
4.10e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 328 EALRQREEMLE---EIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFD----SIRSERDDLREETVKLKEELK 400
Cdd:TIGR02169 288 EQLRVKEKIGEleaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEreieEERKRRDKLTEEYAELKEELE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 401 KhgiiLNSEIATNGETSDTvndvgyqaptkiTKEELNALKsagegtldVRLKKLIDERECLLEQIKKL---KGQLEGRQK 477
Cdd:TIGR02169 368 D----LRAELEEVDKEFAE------------TRDELKDYR--------EKLEKLKREINELKRELDRLqeeLQRLSEELA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 478 NNKLDLLRAEDGILENGTDAHVMDLQ-RDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRyrsaaenAEKIEDELK 556
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK-------LQRELAEAE 496
|
250 260
....*....|....*....|....*
gi 1039727780 557 AEKRKLQRELRSALDKTEELEVSNG 581
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEVLKASIQ 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
322-601 |
1.50e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 322 QFAEVKEALRQRE--EMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEffdSIRSERDDLREETVKLKEEL 399
Cdd:COG1196 214 RYRELKEELKELEaeLLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 400 KKHGI----ILNSEIATNGETSDTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEgR 475
Cdd:COG1196 291 YELLAelarLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL-E 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 476 QKNNKLDLLRAEDGILENgtDAHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDEL 555
Cdd:COG1196 370 AEAELAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1039727780 556 KAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 601
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
236-600 |
6.35e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 6.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 236 TSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMlleleeqlaesqRQYEEKNKEFEREKHA 315
Cdd:pfam15921 485 TAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL------------KNEGDHLRNVQTECEA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 316 hsiLQFQFAE---VKEALRQR-EEMLEEIRQ-------LQQKQAGFIREISD----LQETIEWKDKKIGALERqkeffds 380
Cdd:pfam15921 553 ---LKLQMAEkdkVIEILRQQiENMTQLVGQhgrtagaMQVEKAQLEKEINDrrleLQEFKILKDKKDAKIRE------- 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 381 IRSERDDLREETVKLKEELKKHgiiLNSEIATNGETSDTVNDVgyqaptKITKEELNALKSAGEgtldVRLKKLIDEREC 460
Cdd:pfam15921 623 LEARVSDLELEKVKLVNAGSER---LRAVKDIKQERDQLLNEV------KTSRNELNSLSEDYE----VLKRNFRNKSEE 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 461 LLEQIKKLKGQLEGRQknNKLDLLRAEDGILEnGTDAHVMDLQRDANRQISdlkfklAKSEQeITALEQNVIRLESQVTr 540
Cdd:pfam15921 690 METTTNKLKMQLKSAQ--SELEQTRNTLKSME-GSDGHAMKVAMGMQKQIT------AKRGQ-IDALQSKIQFLEEAMT- 758
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039727780 541 yrsaaeNAEKIEDELKAEKRKLQRELRS-ALDKTE---ELEVSNGHlVKRLEKMKANRSALLSQ 600
Cdd:pfam15921 759 ------NANKEKHFLKEEKNKLSQELSTvATEKNKmagELEVLRSQ-ERRLKEKVANMEVALDK 815
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
324-577 |
1.23e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 324 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETiewKDKKIGALERQKEFFDSIRSERDDLREETVKLKEELKKHG 403
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEK---RDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 404 IILNS---EIATNGETSDTVNDVGYqaPTKITKEELNALksagEGTLDVRLKKLIDEREcLLEQIKKLKGQLEGRQK--- 477
Cdd:COG1340 85 EKLNElreELDELRKELAELNKAGG--SIDKLRKEIERL----EWRQQTEVLSPEEEKE-LVEKIKELEKELEKAKKale 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 478 -NNKLDLLRAE-DGILENGTDAHvMDLQRDANrQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDEL 555
Cdd:COG1340 158 kNEKLKELRAElKELRKEAEEIH-KKIKELAE-EAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIEL 235
|
250 260
....*....|....*....|..
gi 1039727780 556 KAEKRKLQRELRSALDKTEELE 577
Cdd:COG1340 236 QKELRELRKELKKLRKKQRALK 257
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
243-523 |
4.87e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 243 EASIREIKDSLAEVEEKYKKAMVSNAQLDNEktnfmyqVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQfq 322
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAE-------LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE-- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 323 fAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEffdSIRSERDDLREETVKLKEELKKH 402
Cdd:COG1196 309 -ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA---EAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 403 GIILNSEIATNGETSDTVNDVGYQAptKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQKNNKLD 482
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAE--EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1039727780 483 LLRAEDGILENGTDAHVMDLQRDANRQISDLKFKLAKSEQE 523
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
325-556 |
7.27e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 325 EVKEALRQREeMLEEIRQLQQKQAGFIREISDLQETIEWkdkkiGALERQKEFFDSIRSERDDLREETVKLKEELKKHgi 404
Cdd:COG4913 243 ALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAA-----LRLWFAQRRLELLEAELEELRAELARLEAELERL-- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 405 ilnseiatngetsdtvndvgyQAPTKITKEELNALK----SAGEGTLDvRLKKLIDERECLLEQIKKLKGQLEGRQKNNK 480
Cdd:COG4913 315 ---------------------EARLDALREELDELEaqirGNGGDRLE-QLEREIERLERELEERERRRARLEALLAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 481 LDLLRAEDGILENGTDAH------------VMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSA-AEN 547
Cdd:COG4913 373 LPLPASAEEFAALRAEAAallealeeeleaLEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAlAEA 452
|
....*....
gi 1039727780 548 AEKIEDELK 556
Cdd:COG4913 453 LGLDEAELP 461
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
303-410 |
1.04e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.15 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 303 EEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRqlqqkqagfiREISDLQETIEWKDKKIGALERQKEFFDSIR 382
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
|
90 100
....*....|....*....|....*...
gi 1039727780 383 SERDDLREETVKLKEELKKhgiiLNSEI 410
Cdd:COG2433 458 RREIRKDREISRLDREIER----LEREL 481
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
240-595 |
1.28e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.88 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 240 MDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLEleeqlaeSQRQYEEKNKEFEREKHAHSIL 319
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKK-------ALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 320 QFQFAEVKEALRQREEMLEEIRQLQQKQagfirEISDLQETIEWKDKKIGALERQKEFFDSIRSERDDLREEtVKLKEEL 399
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQ-----EIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEE-LKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 400 KKHGIILNSEIATNGETSDTVNDVGYQAPTKITKEELNALKSAGEGTLdvRLKKLIDERECLLEQIKKLKGQLEGRQKNN 479
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKRE--AEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 480 KLDLLRAEDGILENGTDAHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEK 559
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350
....*....|....*....|....*....|....*.
gi 1039727780 560 RKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRS 595
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
352-600 |
1.87e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 352 REISDLQETIEWKDKKIGALERQKEffdSIRSERDDLREETVKLKEELKKhgiilnseiatngetsdtvndvgyqaptki 431
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEK---ALLKQLAALERRIAALARRIRA------------------------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 432 TKEELNALKSagegtldvRLKKLIDERECLLEQIKKLKGQLEGR----QKNNKLDLLRaedgILENGTDAhvmdlqRDAN 507
Cdd:COG4942 74 LEQELAALEA--------ELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPLA----LLLSPEDF------LDAV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 508 RQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRL 587
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
250
....*....|...
gi 1039727780 588 EKMKANRSALLSQ 600
Cdd:COG4942 216 AELQQEAEELEAL 228
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
241-592 |
1.90e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 241 DTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEqlaeSQRQYEEKNKEFEREKHAHSILQ 320
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE----LEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 321 FQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWK---DKKIGALERQKEFFDSIRSERDDLREETVKLKE 397
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELreiEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 398 ELKKhgiiLNSEIATNGETSDTVNDVgyqaptKITKEELNALKSAGEGTLDVRLKKLIDE----RECLLEQIKKL---KG 470
Cdd:PRK03918 346 KLKE----LEKRLEELEERHELYEEA------KAKKEELERLKKRLTGLTPEKLEKELEElekaKEEIEEEISKItarIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 471 QLEGRQKNNKLDL--LRAEDGIL----ENGTDAHVMDLQRDANRQISDLKFKLAKSEQEITALE------QNVIRLESQV 538
Cdd:PRK03918 416 ELKKEIKELKKAIeeLKKAKGKCpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRkelrelEKVLKKESEL 495
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039727780 539 TRYRSAAENAEKIEDELKA----EKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 592
Cdd:PRK03918 496 IKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
324-597 |
1.91e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 324 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEW----------------KDKKIGALERQKEFFDSIRSERDD 387
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgreltEEHRKELLEEYTAELKRIEKELKE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 388 LREETVKLKEELKKHGIILN--SEIATNGETSDTVNDVgYQAPTKITKEELNALKSAGEGTLDvRLKKLIDERECLLEQI 465
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKkeSELIKLKELAEQLKEL-EEKLKKYNLEELEKKAEEYEKLKE-KLIKLKGEIKSLKKEL 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 466 KKLKGqLEGRQK--NNKLDLLRAE----DGILENGTDAHVMDLQ----------------RDANRQISDLKFKLAKSEQE 523
Cdd:PRK03918 549 EKLEE-LKKKLAelEKKLDELEEElaelLKELEELGFESVEELEerlkelepfyneylelKDAEKELEREEKELKKLEEE 627
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039727780 524 ITALEQNVIRLESQVTRYRSAAENAEKIEDE-----LKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSAL 597
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
446-575 |
2.06e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 446 TLDVRLKKLIDERECLLEQIKKLKGQLEGRQK-----NNKLDLLRAEDGILENGTDAHVMDLQRD--------ANRQISD 512
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEArleaaKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrNNKEYEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039727780 513 LKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 575
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
246-577 |
2.14e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 246 IREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAE 325
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 326 VKEALRQREEmleEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIRSERDDLREEtvkLKEELKkhgiI 405
Cdd:TIGR04523 403 QEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES---LETQLK----V 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 406 LNSEIATNGETSDTVndvgyQAPTKITKEELNALKSAGEgTLDVRLKKLIDERECLLEQIKKLKgqLEGRQKNNKLDLLR 485
Cdd:TIGR04523 473 LSRSINKIKQNLEQK-----QKELKSKEKELKKLNEEKK-ELEEKVKDLTKKISSLKEKIEKLE--SEKKEKESKISDLE 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 486 AEDGILENGTDAHVMDLQRDANRQ--------ISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKA 557
Cdd:TIGR04523 545 DELNKDDFELKKENLEKEIDEKNKeieelkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
330 340
....*....|....*....|
gi 1039727780 558 EKRKLQRELRSALDKTEELE 577
Cdd:TIGR04523 625 ENEKLSSIIKNIKSKKNKLK 644
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
327-601 |
2.17e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 327 KEALRQREEMLEEIRQLQQKQAgfireISDLQETIEWKDKKIGALERQKEFFDSIrserDDLREETVKLKEELKKHgiil 406
Cdd:PRK10929 25 EKQITQELEQAKAAKTPAQAEI-----VEALQSALNWLEERKGSLERAKQYQQVI----DNFPKLSAELRQQLNNE---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 407 nseiatngetSDTVNDVgyqaPTKITKEELNalksagEGTLDVRLKKLIDERECLLEQ-----IKKLKGQLEGRQKNNKL 481
Cdd:PRK10929 92 ----------RDEPRSV----PPNMSTDALE------QEILQVSSQLLEKSRQAQQEQdrareISDSLSQLPQQQTEARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 482 DLLRAEDGILENGTDAHVMDLQRDANRQISDLKFKLAKSEQEITAL----EQNVIRLESQVTRYRSaaenaEKIEDELKA 557
Cdd:PRK10929 152 QLNEIERRLQTLGTPNTPLAQAQLTALQAESAALKALVDELELAQLsannRQELARLRSELAKKRS-----QQLDAYLQA 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1039727780 558 EKRKL----QRELRSALDKTEELEVSNGHLVKRL-EKMKANR--SALLSQQ 601
Cdd:PRK10929 227 LRNQLnsqrQREAERALESTELLAEQSGDLPKSIvAQFKINRelSQALNQQ 277
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
324-594 |
3.39e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 324 AEVKEALRQREEMLEEIRQLQQKQAGFI--REISDLQETIEWKDKKIGA--LERQKEFFDSIRSERDDLREETVKLKEEL 399
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLeeLEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 400 KKhGIILNSEIATNGETSDTVndvgyQAPTKITKEELNALKSAGEGTLDVRLKKL--IDERECLLEQIKKLKGQLEGRQK 477
Cdd:PRK03918 549 EK-LEELKKKLAELEKKLDEL-----EEELAELLKELEELGFESVEELEERLKELepFYNEYLELKDAEKELEREEKELK 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 478 NNKLDLLRAEDGILENGTDAhvmdlqRDANRQISDLKFKLakSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKA 557
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRL------EELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
250 260 270
....*....|....*....|....*....|....*..
gi 1039727780 558 EKRKLQRELRSALDKTEELEVsnghLVKRLEKMKANR 594
Cdd:PRK03918 695 TLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
303-493 |
4.82e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 303 EEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIR 382
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 383 sERDDLREETVKLKEELKKhgiiLNSEIATNGETSDTVNDVGYQAptKITKEELNALKSAGEGTLDVRLKKLIDERECLL 462
Cdd:COG4717 133 -ELEALEAELAELPERLEE----LEERLEELRELEEELEELEAEL--AELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|.
gi 1039727780 463 EQIKKLKGQLEgrQKNNKLDLLRAEDGILEN 493
Cdd:COG4717 206 QRLAELEEELE--EAQEELEELEEELEQLEN 234
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
317-493 |
5.09e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 317 SILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQ--ETIEWKDKKIGALER--------QKEFFDSIRSERD 386
Cdd:PRK05771 86 ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYvsvfvgtvPEDKLEELKLESD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 387 DLREETVKLKEE--------LKKHGIILNSEIATNGETSDTVNDVGyqaptkITKEELNALKSagegtldvRLKKLIDER 458
Cdd:PRK05771 166 VENVEYISTDKGyvyvvvvvLKELSDEVEEELKKLGFERLELEEEG------TPSELIREIKE--------ELEEIEKER 231
|
170 180 190
....*....|....*....|....*....|....*
gi 1039727780 459 ECLLEQIKKLKGQLEgrqknnklDLLRAEDGILEN 493
Cdd:PRK05771 232 ESLLEELKELAKKYL--------EELLALYEYLEI 258
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
297-550 |
9.86e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.59 E-value: 9.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 297 ESQRQYEEKNKEFEREKhahsilqfqfaevkealRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKE 376
Cdd:COG4942 31 QLQQEIAELEKELAALK-----------------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 377 ffdSIRSERDDLREETVKLKEELKKHGIILNSEIATNGET-SDTVNDVGY-QAPTKITKEELNALKSAGEgtldvRLKKL 454
Cdd:COG4942 94 ---ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDfLDAVRRLQYlKYLAPARREQAEELRADLA-----ELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727780 455 IDERECLLEQIKKLKGQLEGRQKnnKLDLLRAEdgilengtdahvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRL 534
Cdd:COG4942 166 RAELEAERAELEALLAELEEERA--ALEALKAE------------------RQKLLARLEKELAELAAELAELQQEAEEL 225
|
250
....*....|....*.
gi 1039727780 535 ESQVTRYRSAAENAEK 550
Cdd:COG4942 226 EALIARLEAEAAAAAE 241
|
|
| |
