|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
52-513 |
7.51e-83 |
|
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: 261.55 E-value: 7.51e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 52 MKELERQQKEIyqvqkkyygldtkwgdieqwmedserysrrfrrntsaSDEDERLSVGSRGSLRTNgydgdycgsqslsr 131
Cdd:pfam09738 20 MRELERQQKEV-------------------------------------EENADRVFDMSSSSGADT-------------- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 132 rsgrasmldesslygarrgsacgsrapseygshlnsssrassrassaraspvveerpdkdfaEKGSRNMPSLSAATLASL 211
Cdd:pfam09738 49 --------------------------------------------------------------ASGSPTASTTSAGTLNSL 66
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 212 GGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEE 291
Cdd:pfam09738 67 GGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELRE 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 292 KNKEFEREKHAHSILQFQFAEVKEALRQREEMLEeirqlqqkqagfireisdlqetiewkdkkigalerqkeffdsirse 371
Cdd:pfam09738 147 KNKELERLKRNLRRLQFQLAELKEQLKQRDELIE---------------------------------------------- 180
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 372 rddlreetvklkeelkKHGIILNSEIATNGEtsdTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQ 451
Cdd:pfam09738 181 ----------------KHGLVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDE 241
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907067513 452 IKKLKGQLEGRQ--KNNKLDLLRAEDGILENGTdaHVMDLQRDANRQISDLKFKLAKSEQEITA 513
Cdd:pfam09738 242 VRKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
207-563 |
1.90e-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: 57.37 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 207 TLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQ 286
Cdd:TIGR02168 653 DLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 287 RQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQagfIREISDLQETIewkdkkigalERQKEFFD 366
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA---EAEIEELEAQI----------EQLKEELK 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 367 SIRSERDDLREETVKLKEELKKHGIILNSEIATNGETSDTVNDVGYQAptKITKEELNALKSAGEgTLDVRLKKLIDERE 446
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIE-ELEELIEELESELE 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 447 CLLEQIKKLKGQLEGRQKNnkLDLLRAEdgilENGTDAHVMDLQRDANRqisdLKFKLAKSEQEITALEQNVIRLESQVT 526
Cdd:TIGR02168 877 ALLNERASLEEALALLRSE--LEELSEE----LRELESKRSELRRELEE----LREKLAQLELRLEGLEVRIDNLQERLS 946
|
330 340 350
....*....|....*....|....*....|....*...
gi 1907067513 527 -RYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 563
Cdd:TIGR02168 947 eEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
257-564 |
1.09e-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: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 257 LDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAG 336
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 337 firEISDLQETIEWKDKKIGALERQ--KEFFDSIRSERDDLREETVKLKEELKKHGIILNSEIATNGETSDTVND-VGYQ 413
Cdd:TIGR02169 766 ---RIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElQEQR 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 414 APTKITKEELNALKSAGEGTLDvRLKKLIDERECLLEQIKKLKGQLEGRQKNNKLDLLRAEDGILENGTDAHvmdlqrDA 493
Cdd:TIGR02169 843 IDLKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIE------KK 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 494 NRQISDLKFKLAKSEQEITALEQNVIRLES---QVTRYRSAAENAEKIE------------------------DELKAEK 546
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGEDEEipeEELSLEDVQAELQRVEeeiralepvnmlaiqeyeevlkrlDELKEKR 995
|
330
....*....|....*...
gi 1907067513 547 RKLQRELRSALDKTEELE 564
Cdd:TIGR02169 996 AKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
311-587 |
3.65e-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: 53.52 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 311 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQkefFDSIRSERDDLREETVKLKEELKKhg 390
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER---IAQLSKELTELEAEIEELEERLEE-- 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 391 iiLNSEIATNGETSDTVNDV--GYQAPTKITKEELNALKSAgEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQKNNKl 468
Cdd:TIGR02168 773 --AEEELAEAEAEIEELEAQieQLKEELKALREALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE- 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 469 dllRAEDGILEngtdahvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRK 548
Cdd:TIGR02168 849 ---ELSEDIES-------------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270
....*....|....*....|....*....|....*....
gi 1907067513 549 LQRELrsaldktEELEVSNGHLVKRLEKMKANRSALLSQ 587
Cdd:TIGR02168 913 LRREL-------EELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
291-587 |
2.00e-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: 50.84 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 291 EKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKeffDSIRS 370
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL---KELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 371 ERDDLREETVKLKEELkkhgiilnseiatngetsdtvndvgyqaptkitkEELNALKSagegtlDVRLKKLIDERECLLE 450
Cdd:TIGR02169 766 RIEELEEDLHKLEEAL----------------------------------NDLEARLS------HSRIPEIQAELSKLEE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 451 QIKKLKGQL-EGRQKNNKLDLLRAedgILEngtdahvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYR 529
Cdd:TIGR02169 806 EVSRIEARLrEIEQKLNRLTLEKE---YLE--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907067513 530 SAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQ 587
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
286-564 |
4.56e-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: 49.67 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 286 QRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----RQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQ 361
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 362 KEFFDSIR----SERDDLREETVKLKEELkkhgiilnseiatngeTSDTVNDVGYQAPTKITKEELNALKSAgEGTLDVR 437
Cdd:TIGR02168 318 LEELEAQLeeleSKLDELAEELAELEEKL----------------EELKEELESLEAELEELEAELEELESR-LEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 438 LKKLIDERECLLEQIKKLKGQLEgRQKNNKLDLLRAEDGILENGTDAhvmdLQRDANRQISDLKFKLAKSEQEITALEQN 517
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIE-RLEARLERLEDRRERLQQEIEEL----LKKLEEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1907067513 518 VIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELE 564
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
311-585 |
4.92e-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: 49.68 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 311 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWK-------DKKIGALERQK--------EFFDSIRSER-DD 374
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVkselkelEARIEELEEDLhkleealnDLEARLSHSRiPE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 375 LREETVKLKEELKKHGIILNSeiaTNGETSDTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKK 454
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLRE---IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 455 LKG---QLEGRQKN--NKLDLLRAEDGILENGTDAHVMDLQRdANRQISDLKFKLAKSEQEITALEQNVIRLESQVTryr 529
Cdd:TIGR02169 873 LEAalrDLESRLGDlkKERDELEAQLRELERKIEELEAQIEK-KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE--- 948
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907067513 530 saaenAEKIEDELKAEKRKLQRELRS-------ALDKTEELEVSNGHLVKRLEKMKANRSALL 585
Cdd:TIGR02169 949 -----EELSLEDVQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
315-568 |
7.60e-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: 49.30 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 315 EALRQREEMLE---EIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFD----SIRSERDDLREETVKLKEELK 387
Cdd:TIGR02169 288 EQLRVKEKIGEleaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEreieEERKRRDKLTEEYAELKEELE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 388 KhgiiLNSEIATNGETSDTvndvgyqaptkiTKEELNALKsagegtldVRLKKLIDERECLLEQIKKL---KGQLEGRQK 464
Cdd:TIGR02169 368 D----LRAELEEVDKEFAE------------TRDELKDYR--------EKLEKLKREINELKRELDRLqeeLQRLSEELA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 465 NNKLDLLRAEDGILENGTDAHVMDLQ-RDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRyrsaaenAEKIEDELK 543
Cdd:TIGR02169 424 DLNAAIAGIEAKINELEEEKEDKALEiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK-------LQRELAEAE 496
|
250 260
....*....|....*....|....*
gi 1907067513 544 AEKRKLQRELRSALDKTEELEVSNG 568
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEVLKASIQ 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
309-588 |
2.11e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 309 QFAEVKEALRQRE--EMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEffdSIRSERDDLREETVKLKEEL 386
Cdd:COG1196 214 RYRELKEELKELEaeLLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 387 KKHGI----ILNSEIATNGETSDTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEgR 462
Cdd:COG1196 291 YELLAelarLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL-E 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 463 QKNNKLDLLRAEDGILENgtDAHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDEL 542
Cdd:COG1196 370 AEAELAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907067513 543 KAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 588
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
223-587 |
1.63e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.72 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 223 TSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMlleleeqlaesqRQYEEKNKEFEREKHA 302
Cdd:pfam15921 485 TAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL------------KNEGDHLRNVQTECEA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 303 hsiLQFQFAE---VKEALRQR-EEMLEEIRQ-------LQQKQAGFIREISD----LQETIEWKDKKIGALERqkeffds 367
Cdd:pfam15921 553 ---LKLQMAEkdkVIEILRQQiENMTQLVGQhgrtagaMQVEKAQLEKEINDrrleLQEFKILKDKKDAKIRE------- 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 368 IRSERDDLREETVKLKEELKKHgiiLNSEIATNGETSDTVNDVgyqaptKITKEELNALKSAGEgtldVRLKKLIDEREC 447
Cdd:pfam15921 623 LEARVSDLELEKVKLVNAGSER---LRAVKDIKQERDQLLNEV------KTSRNELNSLSEDYE----VLKRNFRNKSEE 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 448 LLEQIKKLKGQLEGRQknNKLDLLRAEDGILEnGTDAHVMDLQRDANRQISdlkfklAKSEQeITALEQNVIRLESQVTr 527
Cdd:pfam15921 690 METTTNKLKMQLKSAQ--SELEQTRNTLKSME-GSDGHAMKVAMGMQKQIT------AKRGQ-IDALQSKIQFLEEAMT- 758
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907067513 528 yrsaaeNAEKIEDELKAEKRKLQRELRS-ALDKTE---ELEVSNGHlVKRLEKMKANRSALLSQ 587
Cdd:pfam15921 759 ------NANKEKHFLKEEKNKLSQELSTvATEKNKmagELEVLRSQ-ERRLKEKVANMEVALDK 815
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
311-564 |
3.20e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 311 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETiewKDKKIGALERQKEFFDSIRSERDDLREETVKLKEELKKHG 390
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEK---RDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 391 IILNS---EIATNGETSDTVNDVGYqaPTKITKEELNALksagEGTLDVRLKKLIDEREcLLEQIKKLKGQLEGRQK--- 464
Cdd:COG1340 85 EKLNElreELDELRKELAELNKAGG--SIDKLRKEIERL----EWRQQTEVLSPEEEKE-LVEKIKELEKELEKAKKale 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 465 -NNKLDLLRAEDGILENGTDAHVMDLQRDANrQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELK 543
Cdd:COG1340 158 kNEKLKELRAELKELRKEAEEIHKKIKELAE-EAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
250 260
....*....|....*....|.
gi 1907067513 544 AEKRKLQRELRSALDKTEELE 564
Cdd:COG1340 237 KELRELRKELKKLRKKQRALK 257
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
230-510 |
5.65e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 230 EASIREIKDSLAEVEEKYKKAMVSNAQLDNEktnfmyqVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQfq 309
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAE-------LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE-- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 310 fAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEffdSIRSERDDLREETVKLKEELKKH 389
Cdd:COG1196 309 -ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA---EAEEALLEAEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 390 GIILNSEIATNGETSDTVNDVGYQAptKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQKNNKLD 469
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAE--EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1907067513 470 LLRAEDGILENGTDAHVMDLQRDANRQISDLKFKLAKSEQE 510
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
312-543 |
9.51e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 9.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 312 EVKEALRQREeMLEEIRQLQQKQAGFIREISDLQETIEWkdkkiGALERQKEFFDSIRSERDDLREETVKLKEELKKHgi 391
Cdd:COG4913 243 ALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAA-----LRLWFAQRRLELLEAELEELRAELARLEAELERL-- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 392 ilnseiatngetsdtvndvgyQAPTKITKEELNALK----SAGEGTLDvRLKKLIDERECLLEQIKKLKGQLEGRQKNNK 467
Cdd:COG4913 315 ---------------------EARLDALREELDELEaqirGNGGDRLE-QLEREIERLERELEERERRRARLEALLAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 468 LDLLRAEDGILENGTDAH------------VMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSA-AEN 534
Cdd:COG4913 373 LPLPASAEEFAALRAEAAallealeeeleaLEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAlAEA 452
|
....*....
gi 1907067513 535 AEKIEDELK 543
Cdd:COG4913 453 LGLDEAELP 461
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
290-397 |
1.22e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 290 EEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRqlqqkqagfiREISDLQETIEWKDKKIGALERQKEFFDSIR 369
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
|
90 100
....*....|....*....|....*...
gi 1907067513 370 SERDDLREETVKLKEELKKhgiiLNSEI 397
Cdd:COG2433 458 RREIRKDREISRLDREIER----LEREL 481
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
314-588 |
2.27e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 314 KEALRQREEMLEEIRQLQQKQAgfireISDLQETIEWKDKKIGALERQKEFFDSIrserDDLREETVKLKEELKKHgiil 393
Cdd:PRK10929 25 EKQITQELEQAKAAKTPAQAEI-----VEALQSALNWLEERKGSLERAKQYQQVI----DNFPKLSAELRQQLNNE---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 394 nseiatngetSDTVNDVgyqaPTKITKEELNalksagEGTLDVRLKKLIDERECLLEQ-----IKKLKGQLEGRQKNNKL 468
Cdd:PRK10929 92 ----------RDEPRSV----PPNMSTDALE------QEILQVSSQLLEKSRQAQQEQdrareISDSLSQLPQQQTEARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 469 DLLRAEDGILENGTDAHVMDLQRDANRQISDLKFKLAKSEQEITAL----EQNVIRLESQVTRYRSaaenaEKIEDELKA 544
Cdd:PRK10929 152 QLNEIERRLQTLGTPNTPLAQAQLTALQAESAALKALVDELELAQLsannRQELARLRSELAKKRS-----QQLDAYLQA 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1907067513 545 EKRKL----QRELRSALDKTEELEVSNGHLVKRL-EKMKANR--SALLSQQ 588
Cdd:PRK10929 227 LRNQLnsqrQREAERALESTELLAEQSGDLPKSIvAQFKINRelSQALNQQ 277
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
339-584 |
2.93e-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: 40.13 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 339 REISDLQETIEWKDKKIGALERQKEffdSIRSERDDLREETVKLKEELKKhgiilnseiatngetsdtvndvgyqaptki 418
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEK---ALLKQLAALERRIAALARRIRA------------------------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 419 TKEELNALKSagegtldvRLKKLIDERECLLEQIKKLKGQLEGR----QKNNKLDLLRaedgILENGTDAhvmdlqRDAN 494
Cdd:COG4942 74 LEQELAALEA--------ELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPLA----LLLSPEDF------LDAV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 495 RQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRL 574
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
250
....*....|
gi 1907067513 575 EKMKANRSAL 584
Cdd:COG4942 216 AELQQEAEEL 225
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
227-582 |
3.15e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.73 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 227 MDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLEleeqlaeSQRQYEEKNKEFEREKHAHSIL 306
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKK-------ALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 307 QFQFAEVKEALRQREEMLEEIRQLQQKQagfirEISDLQETIEWKDKKIGALERQKEFFDSIRSERDDLREEtVKLKEEL 386
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQ-----EIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEE-LKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 387 KKHGIILNSEIATNGETSDTVNDVGYQAPTKITKEELNALKSAGEGTLdvRLKKLIDERECLLEQIKKLKGQLEGRQKNN 466
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKRE--AEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 467 KLDLLRAEDGILENGTDAHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEK 546
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907067513 547 RKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRS 582
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
433-562 |
3.23e-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: 39.52 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 433 TLDVRLKKLIDERECLLEQIKKLKGQLEGRQK-----NNKLDLLRAEDGILENGTDAHVMDLQRD--------ANRQISD 499
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEArleaaKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrNNKEYEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907067513 500 LKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 562
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
311-584 |
3.81e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 311 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEW----------------KDKKIGALERQKEFFDSIRSERDD 374
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgreltEEHRKELLEEYTAELKRIEKELKE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 375 LREETVKLKEELKKHGIILN--SEIATNGETSDTVNDVgYQAPTKITKEELNALKSAGEGTLDvRLKKLIDERECLLEQI 452
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKkeSELIKLKELAEQLKEL-EEKLKKYNLEELEKKAEEYEKLKE-KLIKLKGEIKSLKKEL 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 453 KKLKGqLEGRQK--NNKLDLLRAE----DGILENGTDAHVMDLQ----------------RDANRQISDLKFKLAKSEQE 510
Cdd:PRK03918 549 EKLEE-LKKKLAelEKKLDELEEElaelLKELEELGFESVEELEerlkelepfyneylelKDAEKELEREEKELKKLEEE 627
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907067513 511 ITALEQNVIRLESQVTRYRSAAENAEKIEDE-----LKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSAL 584
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
438-579 |
3.89e-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: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 438 LKKLIDERECLLEQIKKLKGQLEGRQKNNKLDLLRAEDGILENGTD----------------AHVMDLQRDANRQISDLK 501
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDrleqlereierlerelEERERRRARLEALLAALG 372
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907067513 502 FKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEkieDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 579
Cdd:COG4913 373 LPLPASAEEFAALRAEAAALLEALEEELEALEEAL---AEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
228-579 |
3.98e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 228 DTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEqlaeSQRQYEEKNKEFEREKHAHSILQ 307
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE----LEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 308 FQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWK---DKKIGALERQKEFFDSIRSERDDLREETVKLKE 384
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELreiEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 385 ELKKhgiiLNSEIATNGETSDTVNDVgyqaptKITKEELNALKSAGEGTLDVRLKKLIDE----RECLLEQIKKL---KG 457
Cdd:PRK03918 346 KLKE----LEKRLEELEERHELYEEA------KAKKEELERLKKRLTGLTPEKLEKELEElekaKEEIEEEISKItarIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 458 QLEGRQKNNKLDLLRAEDGILE------NGTDAHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLE------SQV 525
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGKcpvcgrELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEkvlkkeSEL 495
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907067513 526 TRYRSAAENAEKIEDELKA----EKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 579
Cdd:PRK03918 496 IKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
304-480 |
5.30e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 304 SILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQ--ETIEWKDKKIGALER--------QKEFFDSIRSERD 373
Cdd:PRK05771 86 ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYvsvfvgtvPEDKLEELKLESD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 374 DLREETVKLKEE--------LKKHGIILNSEIATNGETSDTVNDVGyqaptkITKEELNALKSagegtldvRLKKLIDER 445
Cdd:PRK05771 166 VENVEYISTDKGyvyvvvvvLKELSDEVEEELKKLGFERLELEEEG------TPSELIREIKE--------ELEEIEKER 231
|
170 180 190
....*....|....*....|....*....|....*
gi 1907067513 446 ECLLEQIKKLKGQLEgrqknnklDLLRAEDGILEN 480
Cdd:PRK05771 232 ESLLEELKELAKKYL--------EELLALYEYLEI 258
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
311-581 |
6.15e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 311 AEVKEALRQREEMLEEIRQLQQKQAGFI--REISDLQETIEWKDKKIGA--LERQKEFFDSIRSERDDLREETVKLKEEL 386
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLeeLEKKAEEYEKLKEKLIKLKGEIKSLKKEL 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 387 KKhGIILNSEIATNGETSDTVndvgyQAPTKITKEELNALKSAGEGTLDVRLKKL--IDERECLLEQIKKLKGQLEGRQK 464
Cdd:PRK03918 549 EK-LEELKKKLAELEKKLDEL-----EEELAELLKELEELGFESVEELEERLKELepFYNEYLELKDAEKELEREEKELK 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 465 NNKLDLLRAEDGILENGTDAhvmdlqRDANRQISDLKFKLakSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKA 544
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRL------EELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAELEELEKRREEIKK 694
|
250 260 270
....*....|....*....|....*....|....*..
gi 1907067513 545 EKRKLQRELRSALDKTEELEVsnghLVKRLEKMKANR 581
Cdd:PRK03918 695 TLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
233-564 |
6.28e-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: 39.62 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 233 IREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAE 312
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 313 VKEALRQREEmleEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIRSERDDLREEtvkLKEELKkhgiI 392
Cdd:TIGR04523 403 QEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES---LETQLK----V 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 393 LNSEIATNGETSDTVndvgyQAPTKITKEELNALKSAGEgTLDVRLKKLIDERECLLEQIKKLKgqLEGRQKNNKLDLLR 472
Cdd:TIGR04523 473 LSRSINKIKQNLEQK-----QKELKSKEKELKKLNEEKK-ELEEKVKDLTKKISSLKEKIEKLE--SEKKEKESKISDLE 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 473 AEDGILENGTDAHVMDLQRDANRQ--------ISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKA 544
Cdd:TIGR04523 545 DELNKDDFELKKENLEKEIDEKNKeieelkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
330 340
....*....|....*....|
gi 1907067513 545 EKRKLQRELRSALDKTEELE 564
Cdd:TIGR04523 625 ENEKLSSIIKNIKSKKNKLK 644
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
290-480 |
6.54e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 290 EEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIR 369
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907067513 370 sERDDLREETVKLKEELKKhgiiLNSEIATNGETSDTVNDVGYQAptKITKEELNALKSAGEGTLDVRLKKLIDERECLL 449
Cdd:COG4717 133 -ELEALEAELAELPERLEE----LEERLEELRELEEELEELEAEL--AELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|.
gi 1907067513 450 EQIKKLKGQLEgrQKNNKLDLLRAEDGILEN 480
Cdd:COG4717 206 QRLAELEEELE--EAQEELEELEEELEQLEN 234
|
|
| |
