|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
52-589 |
1.59e-75 |
|
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: 244.22 E-value: 1.59e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 52 MKELERQQKEIyqvqkkyygldtkwgdieqwmedserysrrfrrntsaSDEDERLSVGSRGSLRAQPeleygspyawtng 131
Cdd:pfam09738 20 MRELERQQKEV-------------------------------------EENADRVFDMSSSSGADTA------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 132 ydgdycgsqslsrrsgrnssfsggdgrvstlsscreeklglscsnlglpssglaskplstqngsrpfvlcnaawptgsyr 211
Cdd:pfam09738 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 212 asmldesslygarrgsacgsrapseygshlnsssrassrassaraspvveerpdkdfaeKGSRNMPSLSAATLASLGGTS 291
Cdd:pfam09738 50 -----------------------------------------------------------SGSPTASTTSAGTLNSLGGTS 70
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 292 SRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKE 371
Cdd:pfam09738 71 SRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKE 150
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 372 FEREKHAHSILQFQFAEVKEALRQREEMLEeirqlqqkqagfireisdlqetiewkdkkigalerqkeffdsirserddl 451
Cdd:pfam09738 151 LERLKRNLRRLQFQLAELKEQLKQRDELIE-------------------------------------------------- 180
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 452 reetvklkeelkKHGIILNSEIATNGEtsdTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKL 531
Cdd:pfam09738 181 ------------KHGLVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKL 245
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 532 KGQLEGRQ--KNNKLDLLRAEDGILENGTdaHVMDLQRDANRQISDLKFKLAKSEQEITA 589
Cdd:pfam09738 246 KLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
283-639 |
1.11e-09 |
|
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: 62.00 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 283 TLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQ 362
Cdd:TIGR02168 653 DLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 363 RQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQagfIREISDLQETIewkdkkigalERQKEFFD 442
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA---EAEIEELEAQI----------EQLKEELK 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 443 SIRSERDDLREETVKLKEELKKHGIILNSEIATNGETSDTVNDVGYQAptKITKEELNALKSAGEgTLDVRLKKLIDERE 522
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIE-ELEELIEELESELE 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 523 CLLEQIKKLKGQLEGRQKNnkLDLLRAEdgilENGTDAHVMDLQRDANRqisdLKFKLAKSEQEITALEQNVIRLESQVT 602
Cdd:TIGR02168 877 ALLNERASLEEALALLRSE--LEELSEE----LRELESKRSELRRELEE----LREKLAQLELRLEGLEVRIDNLQERLS 946
|
330 340 350
....*....|....*....|....*....|....*...
gi 1039727766 603 -RYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 639
Cdd:TIGR02168 947 eEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
310-640 |
3.70e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.08 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 310 REIKDSLAEVEEKYKKamvsnaqLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEV 389
Cdd:TIGR02169 670 RSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 390 KEALRQREEMLEEIRQLQQKQAGfirEISDLQETIEWKDKKIGALERQ--KEFFDSIRSERDDLREETVKLKEELKKHGI 467
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEA---RIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 468 ILNSEIATNGETSDTVND-VGYQAPTKITKEELNALKSAGEGTLDvRLKKLIDERECLLEQIKKLKGQLEGRQKNNKLDL 546
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQElQEQRIDLKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 547 LRAEDGILENGTDAHvmdlqrDANRQISDLKFKLAKSEQEITALEQNVIRLES---QVTRYRSAAENAEKIE-------- 615
Cdd:TIGR02169 899 RELERKIEELEAQIE------KKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeEELSLEDVQAELQRVEeeiralep 972
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1039727766 616 ----------------DELKAEKRKLQRELRSALDKTEELE 640
Cdd:TIGR02169 973 vnmlaiqeyeevlkrlDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
387-663 |
2.16e-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: 57.76 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 387 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQkefFDSIRSERDDLREETVKLKEELKKhg 466
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER---IAQLSKELTELEAEIEELEERLEE-- 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 467 iiLNSEIATNGETSDTVNDV--GYQAPTKITKEELNALKSAgEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQKNNKl 544
Cdd:TIGR02168 773 --AEEELAEAEAEIEELEAQieQLKEELKALREALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE- 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 545 dllRAEDGILEngtdahvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRK 624
Cdd:TIGR02168 849 ---ELSEDIES-------------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270
....*....|....*....|....*....|....*....
gi 1039727766 625 LQRELrsaldktEELEVSNGHLVKRLEKMKANRSALLSQ 663
Cdd:TIGR02168 913 LRREL-------EELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
367-663 |
7.00e-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: 7.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 367 EKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKeffDSIRS 446
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL---KELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 447 ERDDLREETVKLKEELkkhgiilnseiatngetsdtvndvgyqaptkitkEELNALKSagegtlDVRLKKLIDERECLLE 526
Cdd:TIGR02169 766 RIEELEEDLHKLEEAL----------------------------------NDLEARLS------HSRIPEIQAELSKLEE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 527 QIKKLKGQL-EGRQKNNKLDLLRAedgILEngtdahvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYR 605
Cdd:TIGR02169 806 EVSRIEARLrEIEQKLNRLTLEKE---YLE--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039727766 606 SAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQ 663
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
387-661 |
1.52e-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: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 387 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWK-------DKKIGALERQK--------EFFDSIRSER-DD 450
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVkselkelEARIEELEEDLhkleealnDLEARLSHSRiPE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 451 LREETVKLKEELKKHGIILNSeiaTNGETSDTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKK 530
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLRE---IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 531 LKG---QLEGRQKN--NKLDLLRAEDGILENGTDAHVMDLQRdANRQISDLKFKLAKSEQEITALEQNVIRLESQVTryr 605
Cdd:TIGR02169 873 LEAalrDLESRLGDlkKERDELEAQLRELERKIEELEAQIEK-KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE--- 948
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039727766 606 saaenAEKIEDELKAEKRKLQRELRS-------ALDKTEELEVSNGHLVKRLEKMKANRSALL 661
Cdd:TIGR02169 949 -----EELSLEDVQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
304-644 |
2.14e-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: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 304 DTEASIREIKDSLAEVEEKYKKamvSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFErekhahsilq 383
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEK---LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELE---------- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 384 fqfAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQK----EFFDSIRSERDDLREEtvkLK 459
Cdd:TIGR02169 301 ---AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRdkltEEYAELKEELEDLRAE---LE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 460 EELKKHgiilnseiatngetsdtvndvgyqaptKITKEELNALKsagegtldVRLKKLIDERECLLEQIKKL---KGQLE 536
Cdd:TIGR02169 375 EVDKEF---------------------------AETRDELKDYR--------EKLEKLKREINELKRELDRLqeeLQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 537 GRQKNNKLDLLRAEDGILENGTDAHVMDLQ-RDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRyrsaaenAEKIE 615
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK-------LQREL 492
|
330 340
....*....|....*....|....*....
gi 1039727766 616 DELKAEKRKLQRELRSALDKTEELEVSNG 644
Cdd:TIGR02169 493 AEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
362-640 |
3.43e-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: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 362 QRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----RQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQ 437
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 438 KEFFDSIR----SERDDLREETVKLKEELkkhgiilnseiatngeTSDTVNDVGYQAPTKITKEELNALKSAgEGTLDVR 513
Cdd:TIGR02168 318 LEELEAQLeeleSKLDELAEELAELEEKL----------------EELKEELESLEAELEELEAELEELESR-LEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 514 LKKLIDERECLLEQIKKLKGQLEgRQKNNKLDLLRAEDGILENGTDAhvmdLQRDANRQISDLKFKLAKSEQEITALEQN 593
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIE-RLEARLERLEDRRERLQQEIEEL----LKKLEEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1039727766 594 VIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELE 640
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
387-640 |
9.59e-07 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 9.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 387 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETiewKDKKIGALERQKEFFDSIRSERDDLREETVKLKEELKKHG 466
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEK---RDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 467 IILNS---EIATNGETSDTVNDVGYqaPTKITKEELNALksagEGTLDVRLKKLIDEREcLLEQIKKLKGQLEGRQK--- 540
Cdd:COG1340 85 EKLNElreELDELRKELAELNKAGG--SIDKLRKEIERL----EWRQQTEVLSPEEEKE-LVEKIKELEKELEKAKKale 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 541 -NNKLDLLRAE-DGILENGTDAHvMDLQRDANrQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDEL 618
Cdd:COG1340 158 kNEKLKELRAElKELRKEAEEIH-KKIKELAE-EAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIEL 235
|
250 260
....*....|....*....|..
gi 1039727766 619 KAEKRKLQRELRSALDKTEELE 640
Cdd:COG1340 236 QKELRELRKELKKLRKKQRALK 257
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
363-664 |
2.08e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 363 RQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAgfiREISDLQETIEWKDKKIGALERQKEffd 442
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE---LELEEAQAEEYELLAELARLEQDIA--- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 443 SIRSERDDLREETVKLKEELKKhgiiLNSEIATNGETsdtvndvgyqaptkitKEELNALKSAGEGTLDVRLKKLIDERE 522
Cdd:COG1196 306 RLEERRRELEERLEELEEELAE----LEEELEELEEE----------------LEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 523 cLLEQIKKLKGQLEGRQKNNKLDLLRAEDGILEngtdahvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVT 602
Cdd:COG1196 366 -ALLEAEAELAEAEEELEELAEELLEALRAAAE-------------LAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039727766 603 RYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 664
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
299-663 |
4.60e-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: 50.12 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 299 TSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMlleleeqlaesqRQYEEKNKEFEREKHA 378
Cdd:pfam15921 485 TAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL------------KNEGDHLRNVQTECEA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 379 hsiLQFQFAE---VKEALRQR-EEMLEEIRQ-------LQQKQAGFIREISD----LQETIEWKDKKIGALERqkeffds 443
Cdd:pfam15921 553 ---LKLQMAEkdkVIEILRQQiENMTQLVGQhgrtagaMQVEKAQLEKEINDrrleLQEFKILKDKKDAKIRE------- 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 444 IRSERDDLREETVKLKEELKKHgiiLNSEIATNGETSDTVNDVgyqaptKITKEELNALKSAGEgtldVRLKKLIDEREC 523
Cdd:pfam15921 623 LEARVSDLELEKVKLVNAGSER---LRAVKDIKQERDQLLNEV------KTSRNELNSLSEDYE----VLKRNFRNKSEE 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 524 LLEQIKKLKGQLEGRQknNKLDLLRAEDGILEnGTDAHVMDLQRDANRQISdlkfklAKSEQeITALEQNVIRLESQVTr 603
Cdd:pfam15921 690 METTTNKLKMQLKSAQ--SELEQTRNTLKSME-GSDGHAMKVAMGMQKQIT------AKRGQ-IDALQSKIQFLEEAMT- 758
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039727766 604 yrsaaeNAEKIEDELKAEKRKLQRELRS-ALDKTE---ELEVSNGHlVKRLEKMKANRSALLSQ 663
Cdd:pfam15921 759 ------NANKEKHFLKEEKNKLSQELSTvATEKNKmagELEVLRSQ-ERRLKEKVANMEVALDK 815
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
387-660 |
6.98e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 6.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 387 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEW----------------KDKKIGALERQKEFFDSIRSERDD 450
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgreltEEHRKELLEEYTAELKRIEKELKE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 451 LREETVKLKEELKKHGIILN--SEIATNGETSDTVNDVgYQAPTKITKEELNALKSAGEGTLDvRLKKLIDERECLLEQI 528
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKkeSELIKLKELAEQLKEL-EEKLKKYNLEELEKKAEEYEKLKE-KLIKLKGEIKSLKKEL 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 529 KKLKGqLEGRQK--NNKLDLLRAE----DGILENGTDAHVMDLQ----------------RDANRQISDLKFKLAKSEQE 586
Cdd:PRK03918 549 EKLEE-LKKKLAelEKKLDELEEElaelLKELEELGFESVEELEerlkelepfyneylelKDAEKELEREEKELKKLEEE 627
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039727766 587 ITALEQNVIRLESQVTRYRSAAENAEKIEDE-----LKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSAL 660
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
303-658 |
7.22e-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: 46.12 E-value: 7.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 303 MDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLEleeqlaeSQRQYEEKNKEFEREKHAHSIL 382
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKK-------ALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 383 QFQFAEVKEALRQREEMLEEIRQLQQKQagfirEISDLQETIEWKDKKIGALERQKEFFDSIRSERDDLREEtVKLKEEL 462
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQ-----EIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEE-LKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 463 KKHGIILNSEIATNGETSDTVNDVGYQAPTKITKEELNALKSAGEGTLdvRLKKLIDERECLLEQIKKLKGQLEGRQKNN 542
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKRE--AEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 543 KLDLLRAEDGILENGTDAHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEK 622
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350
....*....|....*....|....*....|....*.
gi 1039727766 623 RKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRS 658
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
304-655 |
7.73e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 304 DTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEqlaeSQRQYEEKNKEFEREKHAHSILQ 383
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE----LEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 384 FQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWK---DKKIGALERQKEFFDSIRSERDDLREETVKLKE 460
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELreiEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 461 ELKKhgiiLNSEIATNGETSDTVNDVgyqaptKITKEELNALKSAGEGTLDVRLKKLIDE----RECLLEQIKKL---KG 533
Cdd:PRK03918 346 KLKE----LEKRLEELEERHELYEEA------KAKKEELERLKKRLTGLTPEKLEKELEElekaKEEIEEEISKItarIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 534 QLEGRQKNNKLDL--LRAEDGIL----ENGTDAHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLE------SQV 601
Cdd:PRK03918 416 ELKKEIKELKKAIeeLKKAKGKCpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEkvlkkeSEL 495
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039727766 602 TRYRSAAENAEKIEDELKA----EKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 655
Cdd:PRK03918 496 IKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
306-634 |
7.82e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 7.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 306 EASIREIKDSLAEVEEKYKKAMVSNAQLDNEktnfmyqVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQfq 385
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAE-------LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE-- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 386 fAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIRSERDDLREETVKLKEELKKH 465
Cdd:COG1196 309 -ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 466 giilnseiatngetsdtvndvgYQAPTKITKEELNALKSAGEgtldvRLKKLIDERECLLEQIKKLKGQLEgRQKNNKLD 545
Cdd:COG1196 388 ----------------------LLEALRAAAELAAQLEELEE-----AEEALLERLERLEEELEELEEALA-ELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 546 LLRAEDGILEngTDAHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAE-KIEDELKAEKRK 624
Cdd:COG1196 440 EEEALEEAAE--EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLA 517
|
330
....*....|
gi 1039727766 625 LQRELRSALD 634
Cdd:COG1196 518 GLRGLAGAVA 527
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
309-640 |
1.00e-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: 45.40 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 309 IREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAE 388
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 389 VKEALRQREEmleEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIRSERDDLREEtvkLKEELKkhgiI 468
Cdd:TIGR04523 403 QEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES---LETQLK----V 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 469 LNSEIATNGETSDTVndvgyQAPTKITKEELNALKSAGEgTLDVRLKKLIDERECLLEQIKKLKgqLEGRQKNNKLDLLr 548
Cdd:TIGR04523 473 LSRSINKIKQNLEQK-----QKELKSKEKELKKLNEEKK-ELEEKVKDLTKKISSLKEKIEKLE--SEKKEKESKISDL- 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 549 aEDGILENGTDAHVMDLQ---RDANRQISDLK--FKLAKSEQE-----ITALEQNVIRLESQVTRYRSAAENAEKIEDEL 618
Cdd:TIGR04523 544 -EDELNKDDFELKKENLEkeiDEKNKEIEELKqtQKSLKKKQEekqelIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
330 340
....*....|....*....|..
gi 1039727766 619 KAEKRKLQRELRSALDKTEELE 640
Cdd:TIGR04523 623 KKENEKLSSIIKNIKSKKNKLK 644
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
388-619 |
1.27e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 388 EVKEALRQREeMLEEIRQLQQKQAGFIREISDLQETIEWkdkkiGALERQKEFFDSIRSERDDLREETVKLKEELKKHgi 467
Cdd:COG4913 243 ALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAA-----LRLWFAQRRLELLEAELEELRAELARLEAELERL-- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 468 ilnseiatngetsdtvndvgyQAPTKITKEELNALK----SAGEGTLDvRLKKLIDERECLLEQIKKLKGQLEGRQKNNK 543
Cdd:COG4913 315 ---------------------EARLDALREELDELEaqirGNGGDRLE-QLEREIERLERELEERERRRARLEALLAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 544 LDLLRAEDGILENGTDAH------------VMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSA-AEN 610
Cdd:COG4913 373 LPLPASAEEFAALRAEAAallealeeeleaLEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAlAEA 452
|
....*....
gi 1039727766 611 AEKIEDELK 619
Cdd:COG4913 453 LGLDEAELP 461
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
306-657 |
1.51e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 306 EASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLE--------LEEQLAESQRQYEEKNKEFEREKh 377
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRKELLEEYTAELKRIEKEL- 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 378 ahsilqfqfAEVKEALRQREEMLEEIRQLQQKQAGFI--REISDLQETIEWKDKKIGA--LERQKEFFDSIRSERDDLRE 453
Cdd:PRK03918 469 ---------KEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLeeLEKKAEEYEKLKEKLIKLKG 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 454 ETVKLKEELKKhGIILNSEIATNGETSDTVNdvgyqaptKITKEELNALKSAGEGT---LDVRLKKL--IDERECLLEQI 528
Cdd:PRK03918 540 EIKSLKKELEK-LEELKKKLAELEKKLDELE--------EELAELLKELEELGFESveeLEERLKELepFYNEYLELKDA 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 529 KKLKGQLEGRQKNNKLDLLRAEDGILENGTDAhvmdlqRDANRQISDLKFKLakSEQEITALEQNVIRLESQVTRYRSAA 608
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETEKRL------EELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAEL 682
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1039727766 609 ENAEKIEDELKAEKRKLQRELRSALDKTEELEVsnghLVKRLEKMKANR 657
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
509-638 |
2.50e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 509 TLDVRLKKLIDERECLLEQIKKLKGQLEGRQK-----NNKLDLLRAEDGILENGTDAHVMDLQRD--------ANRQISD 575
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEArleaaKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrNNKEYEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039727766 576 LKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 638
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
415-660 |
2.69e-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: 43.60 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 415 REISDLQETIEWKDKKIGALERQKEffdSIRSERDDLREETVKLKEELKKhgiilnseiatngetsdtvndvgyqaptki 494
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEK---ALLKQLAALERRIAALARRIRA------------------------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 495 TKEELNALKSagegtldvRLKKLIDERECLLEQIKKLKGQLEGR----QKNNKLDLLRaedgILENGTDAhvmdlqRDAN 570
Cdd:COG4942 74 LEQELAALEA--------ELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPLA----LLLSPEDF------LDAV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 571 RQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRL 650
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
250
....*....|
gi 1039727766 651 EKMKANRSAL 660
Cdd:COG4942 216 AELQQEAEEL 225
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
385-664 |
4.50e-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: 4.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 385 QFAEVKEALRQRE--EMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEffdSIRSERDDLREETVKLKEEL 462
Cdd:COG1196 214 RYRELKEELKELEaeLLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 463 kkhgiilnseiatngetsdtvndvgyqaptkitkEELNALKSAGEGTLDVRLKKLIDEREcLLEQIKKLKGQLEGRQKNN 542
Cdd:COG1196 291 ----------------------------------YELLAELARLEQDIARLEERRRELEE-RLEELEEELAELEEELEEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 543 KLDLLRAEDgilengtdahvmdlqrdanrqisdlkfKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEK 622
Cdd:COG1196 336 EEELEELEE---------------------------ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1039727766 623 RKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 664
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
366-473 |
5.14e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 366 EEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRqlqqkqagfiREISDLQETIEWKDKKIGALERQKEFFDSIR 445
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
|
90 100
....*....|....*....|....*...
gi 1039727766 446 SERDDLREETVKLKEELKKhgiiLNSEI 473
Cdd:COG2433 458 RREIRKDREISRLDREIER----LEREL 481
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
366-556 |
5.65e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 366 EEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIR 445
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 446 sERDDLREETVKLKEELKKhgiiLNSEIATNGETSDTVNDVGYQAptKITKEELNALKSAGEGTLDVRLKKLIDERECLL 525
Cdd:COG4717 133 -ELEALEAELAELPERLEE----LEERLEELRELEEELEELEAEL--AELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|.
gi 1039727766 526 EQIKKLKGQLEgrQKNNKLDLLRAEDGILEN 556
Cdd:COG4717 206 QRLAELEEELE--EAQEELEELEEELEQLEN 234
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
382-654 |
8.60e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 8.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 382 LQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIRSERDDLREETVKLKEE 461
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 462 LKKHGIILnseiatnGETSDTVNDVgyQAPTKITKEELNALKS-AGEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQK 540
Cdd:PRK03918 254 KRKLEEKI-------RELEERIEEL--KKEIEELEEKVKELKElKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 541 NNKLDLLRAEdgilengtdahvmdlqrDANRQISDLKFKLAKSEQEITALE------QNVIRLESQVTRYRS--AAENAE 612
Cdd:PRK03918 325 GIEERIKELE-----------------EKEERLEELKKKLKELEKRLEELEerhelyEEAKAKKEELERLKKrlTGLTPE 387
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1039727766 613 KIEDELK-AEKRK--LQRELRSALDKTEELEVSNGHLVKRLEKMK 654
Cdd:PRK03918 388 KLEKELEeLEKAKeeIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
362-664 |
1.04e-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: 42.31 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 362 QRQYEEKNKEFEREKHAHSILQFQFAEVK---EALRQR--EEMLEEIR-QLQQKQagfiREISDLQETIEWKDKKIGALE 435
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEKQLNQLKseiSDLNNQkeQDWNKELKsELKNQE----KKLEEIQNQISQNNKIISQLN 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 436 RQKEffdSIRSERDDLREETVKLKEELKKHGIILNSEIATNGETSDTVNDVGYQA---PTKITK-EELNALKsagegtlD 511
Cdd:TIGR04523 342 EQIS---QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIndlESKIQNqEKLNQQK-------D 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 512 VRLKKLIDERECLLEQIKKLKGQLEgrQKNNKLDLLRAEDGILE---NGTDAHVMDLQ---RDANRQISDLKFKLAKSEQ 585
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETII--KNNSEIKDLTNQDSVKEliiKNLDNTRESLEtqlKVLSRSINKIKQNLEQKQK 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 586 EITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRE----------LRSALD------KTEELEVSNGHLVKR 649
Cdd:TIGR04523 490 ELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEkkekeskisdLEDELNkddfelKKENLEKEIDEKNKE 569
|
330
....*....|....*
gi 1039727766 650 LEKMKANRSALLSQQ 664
Cdd:TIGR04523 570 IEELKQTQKSLKKKQ 584
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
364-655 |
1.43e-03 |
|
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: 41.97 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 364 QYEEKNKEFEREKHAHSILQFQFAEvkealRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEffdS 443
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEELR-----EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE---E 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 444 IRSERDDLREETVKLKEELKkhgiilnseiatngetsdtvndvgyqaptkITKEELNALKSAGEgTLDVRLKKLIDEREC 523
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQ------------------------------ILRERLANLERQLE-ELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 524 LLEQIKKLKGQLEGRQKN-----NKLDLLRAEDGILENGtdahvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLE 598
Cdd:TIGR02168 335 LAEELAELEEKLEELKEElesleAELEELEAELEELESR--------LEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039727766 599 SQVT-----RYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 655
Cdd:TIGR02168 407 ARLErledrRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
390-664 |
1.43e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.96 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 390 KEALRQREEMLEEIRQLQQKQAgfireISDLQETIEWKDKKIGALERQKEFFDSIrserDDLREETVKLKEELKKHgiil 469
Cdd:PRK10929 25 EKQITQELEQAKAAKTPAQAEI-----VEALQSALNWLEERKGSLERAKQYQQVI----DNFPKLSAELRQQLNNE---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 470 nseiatngetSDTVNDVgyqaPTKITKEELNalksagEGTLDVRLKKLIDERECLLEQ-----IKKLKGQLEGRQKNNKL 544
Cdd:PRK10929 92 ----------RDEPRSV----PPNMSTDALE------QEILQVSSQLLEKSRQAQQEQdrareISDSLSQLPQQQTEARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 545 DLLRAEDGILENGTDAHVMDLQRDANRQISDLKFKLAKSEQEITAL----EQNVIRLESQVTRYRSaaenaEKIEDELKA 620
Cdd:PRK10929 152 QLNEIERRLQTLGTPNTPLAQAQLTALQAESAALKALVDELELAQLsannRQELARLRSELAKKRS-----QQLDAYLQA 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1039727766 621 EKRKL----QRELRSALDKTEELEVSNGHLVKRL-EKMKANR--SALLSQQ 664
Cdd:PRK10929 227 LRNQLnsqrQREAERALESTELLAEQSGDLPKSIvAQFKINRelSQALNQQ 277
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
360-613 |
1.43e-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: 41.29 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 360 ESQRQYEEKNKEFEREKhahsilqfqfaevkealRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKE 439
Cdd:COG4942 31 QLQQEIAELEKELAALK-----------------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 440 ffdSIRSERDDLREETVKLKEELKKHGIILNSEIATNGET-SDTVNDVGY-QAPTKITKEELNALKSAGEgtldvRLKKL 517
Cdd:COG4942 94 ---ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDfLDAVRRLQYlKYLAPARREQAEELRADLA-----ELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 518 IDERECLLEQIKKLKGQLEGRQKnnKLDLLRAEdgilengtdahvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRL 597
Cdd:COG4942 166 RAELEAERAELEALLAELEEERA--ALEALKAE------------------RQKLLARLEKELAELAAELAELQQEAEEL 225
|
250
....*....|....*.
gi 1039727766 598 ESQVTRYRSAAENAEK 613
Cdd:COG4942 226 EALIARLEAEAAAAAE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
304-639 |
2.13e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 304 DTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES--QRQYEEKNKEFEREKHAHSI 381
Cdd:COG4717 85 EKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAelPERLEELEERLEELRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 382 LQFQFAEVKEALRQREEMLEEIRQLQQKQ-AGFIREISDLQETIEWKDKKIGALERQKEffdSIRSERDDLREETV--KL 458
Cdd:COG4717 165 LEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE---ELEEELEQLENELEaaAL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 459 KEELKKHGIILNSEIAtngetsdTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEGR 538
Cdd:COG4717 242 EERLKEARLLLLIAAA-------LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 539 Q-KNNKLDLLRAEDGILENGTDAHVMDLQrdanRQISDLKFKLAKSEQEITALEQNVIRLESQ----------VTRYRSA 607
Cdd:COG4717 315 ElEEEELEELLAALGLPPDLSPEELLELL----DRIEELQELLREAEELEEELQLEELEQEIAallaeagvedEEELRAA 390
|
330 340 350
....*....|....*....|....*....|..
gi 1039727766 608 AENAEKIEdELKAEKRKLQRELRSALDKTEEL 639
Cdd:COG4717 391 LEQAEEYQ-ELKEELEELEEQLEELLGELEEL 421
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
332-655 |
2.78e-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: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 332 QLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREkhahsiLQFQFAEVKEALRQREEMLEEI----RQLQ 407
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQ------LVLANSELTEARTERDQFSQESgnldDQLQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 408 QKQAGFIREISDLQETIEwKDKKIGALERQKEF-FDSIRSERDDLREETVKLKEELKkhgiilnseiatngetsdtvndv 486
Cdd:pfam15921 381 KLLADLHKREKELSLEKE-QNKRLWDRDTGNSItIDHLRRELDDRNMEVQRLEALLK----------------------- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 487 gyqaptkitkeelnALKSAGEGTLDVRLKKLIDEREClLEQIKKLKGQLEGRQknnklDLLRAedgILENGTdAHVMDLQ 566
Cdd:pfam15921 437 --------------AMKSECQGQMERQMAAIQGKNES-LEKVSSLTAQLESTK-----EMLRK---VVEELT-AKKMTLE 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 567 rDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELK-------------AEKRKLQRELRSAL 633
Cdd:pfam15921 493 -SSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRnvqtecealklqmAEKDKVIEILRQQI 571
|
330 340
....*....|....*....|..
gi 1039727766 634 DKTEELEVSNGHLVKRLEKMKA 655
Cdd:pfam15921 572 ENMTQLVGQHGRTAGAMQVEKA 593
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
306-664 |
3.00e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 306 EASIREIKDSLAEVEEKYKKamvsnaqLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNK-------EFEREKha 378
Cdd:TIGR04523 81 EQQIKDLNDKLKKNKDKINK-------LNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKnidkfltEIKKKE-- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 379 hsilqfqfAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIewkdKKIGALERQKEFFDSIRSERDDLREETVKL 458
Cdd:TIGR04523 152 --------KELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI----DKIKNKLLKLELLLSNLKKKIQKNKSLESQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 459 KEELKKHGIILNSEIATNgetSDTVNDVgyQAPTKITKEELNALKSAGEGTLD---------VRLKKLIDEREcllEQIK 529
Cdd:TIGR04523 220 ISELKKQNNQLKDNIEKK---QQEINEK--TTEISNTQTQLNQLKDEQNKIKKqlsekqkelEQNNKKIKELE---KQLN 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 530 KLKGQLEGRQKNNKLDLLRAEDGILENgTDAHVMDLQ---RDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRS 606
Cdd:TIGR04523 292 QLKSEISDLNNQKEQDWNKELKSELKN-QEKKLEEIQnqiSQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN 370
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039727766 607 AAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 664
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
428-642 |
3.37e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 428 DKKIGALERQKEFFDS-IRSERDDLREETVKLKEELKKHGII-LNSEIATNGETSDTVND--VGYQAPTKITKEELNALK 503
Cdd:COG3206 167 ELRREEARKALEFLEEqLPELRKELEEAEAALEEFRQKNGLVdLSEEAKLLLQQLSELESqlAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 504 SAGEGTLDVRLKKLIDEreclleQIKKLKGQLegrqknnkLDLLRAEDGILENGTDAH--VMDLQR---DANRQISD-LK 577
Cdd:COG3206 247 AQLGSGPDALPELLQSP------VIQQLRAQL--------AELEAELAELSARYTPNHpdVIALRAqiaALRAQLQQeAQ 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039727766 578 FKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELkaekRKLQRELRSA-------LDKTEELEVS 642
Cdd:COG3206 313 RILASLEAELEALQAREASLQAQLAQLEARLAELPELEAEL----RRLEREVEVArelyeslLQRLEEARLA 380
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
380-633 |
3.39e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 380 SILQFQFAEVKEALRQREEMLEeiRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIRSERDDLREETVKLK 459
Cdd:COG4717 38 TLLAFIRAMLLERLEKEADELF--KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 460 EELKKHGIILNseiatngetsdtvndvgyQAPTKITKEELNALKSAGEGTLDvRLKKLIDERECLLEQIKKLKGQLEgrQ 539
Cdd:COG4717 116 EELEKLEKLLQ------------------LLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAELA--E 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 540 KNNKLDLLRAEDGIlengtdahvmdlqrDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKiEDELK 619
Cdd:COG4717 175 LQEELEELLEQLSL--------------ATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAA 239
|
250
....*....|....
gi 1039727766 620 AEKRKLQRELRSAL 633
Cdd:COG4717 240 ALEERLKEARLLLL 253
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
380-556 |
3.91e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 380 SILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQ--ETIEWKDKKIGALER--------QKEFFDSIRSERD 449
Cdd:PRK05771 86 ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYvsvfvgtvPEDKLEELKLESD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 450 DLREETVKLKEE--------LKKHGIILNSEIATNGETSDTVNDVGyqaptkITKEELNALKSagegtldvRLKKLIDER 521
Cdd:PRK05771 166 VENVEYISTDKGyvyvvvvvLKELSDEVEEELKKLGFERLELEEEG------TPSELIREIKE--------ELEEIEKER 231
|
170 180 190
....*....|....*....|....*....|....*
gi 1039727766 522 ECLLEQIKKLKGQLEgrqknnklDLLRAEDGILEN 556
Cdd:PRK05771 232 ESLLEELKELAKKYL--------EELLALYEYLEI 258
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
500-664 |
4.37e-03 |
|
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: 40.43 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 500 NALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEG--RQKNN---KLDLLRAEDGILENGTDAHVMDLQ------RD 568
Cdd:TIGR02168 220 AELRELELALLVLRLEELREELEELQEELKEAEEELEEltAELQEleeKLEELRLEVSELEEEIEELQKELYalaneiSR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 569 ANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVK 648
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
170
....*....|....*.
gi 1039727766 649 RLEKMKANRSALLSQQ 664
Cdd:TIGR02168 380 QLETLRSKVAQLELQI 395
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
392-590 |
4.93e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 392 ALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFF------DSIRSERDDLREETVKLKEElkkh 465
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDAS---- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 466 giilNSEIATNGETSDTVndvgyqaptkitKEELNALKSAgEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQKNNKLD 545
Cdd:COG4913 684 ----SDDLAALEEQLEEL------------EAELEELEEE-LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039727766 546 L-LRAEDGILENGTDAHVMDLQRDANRQISDLKFKLAKSEQEITAL 590
Cdd:COG4913 747 LrALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
386-663 |
5.82e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 39.82 E-value: 5.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 386 FAEVKEALRQREEMLEEIRQLQQ-KQAGFIREISDLQETIEWKDKKI--------GALERQKEFFDSIRSERDdlreetv 456
Cdd:pfam12128 595 WAASEEELRERLDKAEEALQSAReKQAAAEEQLVQANGELEKASREEtfartalkNARLDLRRLFDEKQSEKD------- 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 457 KLKEELKKHGIILNSEIaTNGETSDTVNDVGYQAPTKITKEEL-------NALKSAGEGTLDVRLKKLIDERECLLEQik 529
Cdd:pfam12128 668 KKNKALAERKDSANERL-NSLEAQLKQLDKKHQAWLEEQKEQKreartekQAYWQVVEGALDAQLALLKAAIAARRSG-- 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 530 kLKGQLEGRQKNNKLDLL-RAEDGILENGTDAHVMDLQRDANR---------------------QISDLKFKLAKSEQEI 587
Cdd:pfam12128 745 -AKAELKALETWYKRDLAsLGVDPDVIAKLKREIRTLERKIERiavrrqevlryfdwyqetwlqRRPRLATQLSNIERAI 823
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 588 TALEQNVIRLESQVTRYRSAAEN----AEKIEDELKAEKRKLQRELRS----ALDKT-EELEVSNGHLVKRLEKMKANRS 658
Cdd:pfam12128 824 SELQQQLARLIADTKLRRAKLEMerkaSEKQQVRLSENLRGLRCEMSKlatlKEDANsEQAQGSIGERLAQLEDLKLKRD 903
|
....*
gi 1039727766 659 ALLSQ 663
Cdd:pfam12128 904 YLSES 908
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
605-664 |
6.70e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 38.75 E-value: 6.70e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 605 RSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 664
Cdd:pfam11932 27 AAAAQSQKKI-DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQI 85
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-453 |
6.75e-03 |
|
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: 39.65 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 304 DTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDmlleleeQLAESQRQYEEKNKEFEREKHAHSILQ 383
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES-------KRSELRRELEELREKLAQLELRLEGLE 935
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039727766 384 FQFAEVKEALRQREEM-LEEIRQLQQKQAGFIREISDLQETIEWKDKKIGA--------LERQKEFFDSIRSERDDLRE 453
Cdd:TIGR02168 936 VRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEARRRLKRLENKIKELGPvnlaaieeYEELKERYDFLTAQKEDLTE 1014
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
309-652 |
8.23e-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: 39.32 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 309 IREIKDSLAEVEEKYK-----------KAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFE---R 374
Cdd:pfam05483 263 LEESRDKANQLEEKTKlqdenlkelieKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEelnK 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 375 EKHAHSILQFQF----AEVKEALRQREEMLEEIR-QLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIRSERD 449
Cdd:pfam05483 343 AKAAHSFVVTEFeattCSLEELLRTEQQRLEKNEdQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLD 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 450 DlREETVKLKEELKKhgiilnseiatngetsdtvndvgyqaptkiTKEELNALKSAGEGT---LDVRLKKLIDERECLLE 526
Cdd:pfam05483 423 E-KKQFEKIAEELKG------------------------------KEQELIFLLQAREKEihdLEIQLTAIKTSEEHYLK 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 527 QIKKLKGQLEGRQKNNKLDLLRAEDGILENgtdahvmdlqRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVtryRS 606
Cdd:pfam05483 472 EVEDLKTELEKEKLKNIELTAHCDKLLLEN----------KELTQEASDMTLELKKHQEDIINCKKQEERMLKQI---EN 538
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1039727766 607 AAENAEKIEDELKAEKRKLQR---ELRSALDKTEELEVSNGHLVKRLEK 652
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFIQkgdEVKCKLDKSEENARSIEYEVLKKEK 587
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
377-620 |
9.51e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 38.66 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 377 HAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERqkeffdsirsERDDLREETV 456
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----------EIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 457 KLKEELKKhgiiLNSEIATNGETSDTVNDVgyqaptkitkeeLNAlKSAGEgTLD--VRLKKLIDERECLLEQIKKLKGQ 534
Cdd:COG3883 83 ERREELGE----RARALYRSGGSVSYLDVL------------LGS-ESFSD-FLDrlSALSKIADADADLLEELKADKAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 535 LEGRQK--NNKLDLLRAEDGILEngtdahvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAE 612
Cdd:COG3883 145 LEAKKAelEAKLAELEALKAELE--------AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
....*...
gi 1039727766 613 KIEDELKA 620
Cdd:COG3883 217 AAAAAAAA 224
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
365-661 |
9.82e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.26 E-value: 9.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 365 YEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSI 444
Cdd:TIGR00606 198 QGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 445 RSERDDLREETVKLKEELKKHgiilnseiatngeTSDTVNDV-GYQAPTKITKEELNALKSAGEGTLDVRLKKLIDEREC 523
Cdd:TIGR00606 278 KKQMEKDNSELELKMEKVFQG-------------TDEQLNDLyHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727766 524 LLEQIKKLKGQLEGRQKNN-KLDLLRaedgiLENGTDAHVMDLQRDA--NRQISD-LKFKLAKSEQEITALEQNVIRLES 599
Cdd:TIGR00606 345 LLVEQGRLQLQADRHQEHIrARDSLI-----QSLATRLELDGFERGPfsERQIKNfHTLVIERQEDEAKTAAQLCADLQS 419
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039727766 600 QVtryRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEvsngHLVKRLEKMKANRSALL 661
Cdd:TIGR00606 420 KE---RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELK----FVIKELQQLEGSSDRIL 474
|
|
| |
