|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
52-552 |
3.34e-79 |
|
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: 253.08 E-value: 3.34e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 52 MKELERQQKEIyqvqkkyygldtkwgdieqwmedserysrrfrrntsaSDEDERLSVGSRGSLRAQPeleygspyawtng 131
Cdd:pfam09738 20 MRELERQQKEV-------------------------------------EENADRVFDMSSSSGADTA------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 132 ydgdycgsqslsrrsgrglscsnlglpssglaskplstqngsrasmldesslygarrgsacgsrapseygshlnsssras 211
Cdd:pfam09738 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 212 srassaraspvveerpdkdfaeKGSRNMPSLSAATLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMV 291
Cdd:pfam09738 50 ----------------------SGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMI 107
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 292 SNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEeirqlqq 371
Cdd:pfam09738 108 SNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIE------- 180
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 372 kqagfireisdlqetiewkdkkigalerqkeffdsirserddlreetvklkeelkKHGIILNSEIATNGEtsdTVNDVGY 451
Cdd:pfam09738 181 -------------------------------------------------------KHGLVIVPDENTNGE---EENSPAD 202
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 452 QAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQ--KNNKLDLLRAEDGILENGTdaHVMDLQ 529
Cdd:pfam09738 203 AKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQ 280
|
490 500
....*....|....*....|...
gi 1039727776 530 RDANRQISDLKFKLAKSEQEITA 552
Cdd:pfam09738 281 REANKQISDYKFKLQKAEQEITT 303
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
246-602 |
3.98e-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: 60.07 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 246 TLASLGGTSSRRGSGDTSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQ 325
Cdd:TIGR02168 653 DLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 326 RQYEEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAgfiREISDLQETIewkdkkigalERQKEFFD 405
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAE---AEIEELEAQI----------EQLKEELK 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 406 SIRSERDDLREETVKLKEELKKHGIILNSEIATNGETSDTVNDVGYQAptKITKEELNALKSAGEgTLDVRLKKLIDERE 485
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIE-ELEELIEELESELE 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 486 CLLEQIKKLKGQLEGRQKNnkLDLLRAEdgilENGTDAHVMDLQRDANRqisdLKFKLAKSEQEITALEQNVIRLESQVT 565
Cdd:TIGR02168 877 ALLNERASLEEALALLRSE--LEELSEE----LRELESKRSELRRELEE----LREKLAQLELRLEGLEVRIDNLQERLS 946
|
330 340 350
....*....|....*....|....*....|....*...
gi 1039727776 566 -RYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 602
Cdd:TIGR02168 947 eEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
273-603 |
1.87e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 273 REIKDSLAEVEEKYKKamvsnaqLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAEV 352
Cdd:TIGR02169 670 RSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 353 KEALRQREEMLEEIRQLQQKQAGfirEISDLQETIEWKDKKIGALERQ--KEFFDSIRSERDDLREETVKLKEELKKHGI 430
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEA---RIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 431 ILNSEIATNGETSDTVND-VGYQAPTKITKEELNALKSAGEGTLDvRLKKLIDERECLLEQIKKLKGQLEGRQKNNKLDL 509
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQElQEQRIDLKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQL 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 510 LRAEDGILENGTDAHvmdlqrDANRQISDLKFKLAKSEQEITALEQNVIRLES---QVTRYRSAAENAEKIE-------- 578
Cdd:TIGR02169 899 RELERKIEELEAQIE------KKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeEELSLEDVQAELQRVEeeiralep 972
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1039727776 579 ----------------DELKAEKRKLQRELRSALDKTEELE 603
Cdd:TIGR02169 973 vnmlaiqeyeevlkrlDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
350-626 |
8.89e-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: 55.45 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 350 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQkefFDSIRSERDDLREETVKLKEELKKhg 429
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER---IAQLSKELTELEAEIEELEERLEE-- 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 430 iiLNSEIATNGETSDTVNDV--GYQAPTKITKEELNALKSAgEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQKNNKl 507
Cdd:TIGR02168 773 --AEEELAEAEAEIEELEAQieQLKEELKALREALDELRAE-LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE- 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 508 dllRAEDGILEngtdahvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRK 587
Cdd:TIGR02168 849 ---ELSEDIES-------------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
|
250 260 270
....*....|....*....|....*....|....*....
gi 1039727776 588 LQRELrsaldktEELEVSNGHLVKRLEKMKANRSALLSQ 626
Cdd:TIGR02168 913 LRREL-------EELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
330-626 |
3.25e-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: 53.53 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 330 EKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKeffDSIRS 409
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSEL---KELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 410 ERDDLREETVKLKEELkkhgiilnseiatngetsdtvndvgyqaptkitkEELNALKSagegtlDVRLKKLIDERECLLE 489
Cdd:TIGR02169 766 RIEELEEDLHKLEEAL----------------------------------NDLEARLS------HSRIPEIQAELSKLEE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 490 QIKKLKGQL-EGRQKNNKLDLLRAedgILEngtdahvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYR 568
Cdd:TIGR02169 806 EVSRIEARLrEIEQKLNRLTLEKE---YLE--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039727776 569 SAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQ 626
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
350-624 |
7.71e-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: 52.38 E-value: 7.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 350 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWK-------DKKIGALERQK--------EFFDSIRSER-DD 413
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVkselkelEARIEELEEDLhkleealnDLEARLSHSRiPE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 414 LREETVKLKEELKKHGIILNSeiaTNGETSDTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKK 493
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLRE---IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 494 LKG---QLEGRQKN--NKLDLLRAEDGILENGTDAHVMDLQRdANRQISDLKFKLAKSEQEITALEQNVIRLESQVTryr 568
Cdd:TIGR02169 873 LEAalrDLESRLGDlkKERDELEAQLRELERKIEELEAQIEK-KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE--- 948
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039727776 569 saaenAEKIEDELKAEKRKLQRELRS-------ALDKTEELEVSNGHLVKRLEKMKANRSALL 624
Cdd:TIGR02169 949 -----EELSLEDVQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
325-603 |
1.14e-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: 51.98 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 325 QRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----RQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQ 400
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 401 KEFFDSIR----SERDDLREETVKLKEELkkhgiilnseiatngeTSDTVNDVGYQAPTKITKEELNALKSAgEGTLDVR 476
Cdd:TIGR02168 318 LEELEAQLeeleSKLDELAEELAELEEKL----------------EELKEELESLEAELEELEAELEELESR-LEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 477 LKKLIDERECLLEQIKKLKGQLEgRQKNNKLDLLRAEDGILENGTDAhvmdLQRDANRQISDLKFKLAKSEQEITALEQN 556
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIE-RLEARLERLEDRRERLQQEIEEL----LKKLEEAELKELQAELEELEEELEELQEE 455
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1039727776 557 VIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELE 603
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
267-607 |
1.21e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 267 DTEASIREIKDSLAEVEEKYKKamvSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFErekhahsilq 346
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEK---LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELE---------- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 347 fqfAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQK----EFFDSIRSERDDLREEtvkLK 422
Cdd:TIGR02169 301 ---AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRdkltEEYAELKEELEDLRAE---LE 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 423 EELKKHgiilnseiatngetsdtvndvgyqaptKITKEELNALKsagegtldVRLKKLIDERECLLEQIKKL---KGQLE 499
Cdd:TIGR02169 375 EVDKEF---------------------------AETRDELKDYR--------EKLEKLKREINELKRELDRLqeeLQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 500 GRQKNNKLDLLRAEDGILENGTDAHVMDLQ-RDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRyrsaaenAEKIE 578
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK-------LQREL 492
|
330 340
....*....|....*....|....*....
gi 1039727776 579 DELKAEKRKLQRELRSALDKTEELEVSNG 607
Cdd:TIGR02169 493 AEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
348-627 |
7.01e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 7.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 348 QFAEVKEALRQRE--EMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEffdSIRSERDDLREETVKLKEEL 425
Cdd:COG1196 214 RYRELKEELKELEaeLLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 426 KKHGI----ILNSEIATNGETSDTVNDVGYQAPTKITKEELNALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEgR 501
Cdd:COG1196 291 YELLAelarLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL-E 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 502 QKNNKLDLLRAEDGILENgtDAHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDEL 581
Cdd:COG1196 370 AEAELAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1039727776 582 KAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 627
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
350-603 |
1.45e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 350 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETiewKDKKIGALERQKEFFDSIRSERDDLREETVKLKEELKKHG 429
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEK---RDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 430 IILNS---EIATNGETSDTVNDVGYqaPTKITKEELNALksagEGTLDVRLKKLIDEREcLLEQIKKLKGQLEGRQK--- 503
Cdd:COG1340 85 EKLNElreELDELRKELAELNKAGG--SIDKLRKEIERL----EWRQQTEVLSPEEEKE-LVEKIKELEKELEKAKKale 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 504 -NNKLDLLRAE-DGILENGTDAHvMDLQRDANrQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDEL 581
Cdd:COG1340 158 kNEKLKELRAElKELRKEAEEIH-KKIKELAE-EAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIEL 235
|
250 260
....*....|....*....|..
gi 1039727776 582 KAEKRKLQRELRSALDKTEELE 603
Cdd:COG1340 236 QKELRELRKELKKLRKKQRALK 257
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
262-626 |
2.57e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 262 TSISMDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMlleleeqlaesqRQYEEKNKEFEREKHA 341
Cdd:pfam15921 485 TAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHL------------KNEGDHLRNVQTECEA 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 342 hsiLQFQFAE---VKEALRQR-EEMLEEIRQ-------LQQKQAGFIREISD----LQETIEWKDKKIGALERqkeffds 406
Cdd:pfam15921 553 ---LKLQMAEkdkVIEILRQQiENMTQLVGQhgrtagaMQVEKAQLEKEINDrrleLQEFKILKDKKDAKIRE------- 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 407 IRSERDDLREETVKLKEELKKHgiiLNSEIATNGETSDTVNDVgyqaptKITKEELNALKSAGEgtldVRLKKLIDEREC 486
Cdd:pfam15921 623 LEARVSDLELEKVKLVNAGSER---LRAVKDIKQERDQLLNEV------KTSRNELNSLSEDYE----VLKRNFRNKSEE 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 487 LLEQIKKLKGQLEGRQknNKLDLLRAEDGILEnGTDAHVMDLQRDANRQISdlkfklAKSEQeITALEQNVIRLESQVTr 566
Cdd:pfam15921 690 METTTNKLKMQLKSAQ--SELEQTRNTLKSME-GSDGHAMKVAMGMQKQIT------AKRGQ-IDALQSKIQFLEEAMT- 758
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039727776 567 yrsaaeNAEKIEDELKAEKRKLQRELRS-ALDKTE---ELEVSNGHlVKRLEKMKANRSALLSQ 626
Cdd:pfam15921 759 ------NANKEKHFLKEEKNKLSQELSTvATEKNKmagELEVLRSQ-ERRLKEKVANMEVALDK 815
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
269-597 |
2.23e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 269 EASIREIKDSLAEVEEKYKKAMVSNAQLDNEktnfmyqVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQfq 348
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAE-------LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE-- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 349 fAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIRSERDDLREETVKLKEELKKH 428
Cdd:COG1196 309 -ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 429 giilnseiatngetsdtvndvgYQAPTKITKEELNALKSAGEgtldvRLKKLIDERECLLEQIKKLKGQLEgRQKNNKLD 508
Cdd:COG1196 388 ----------------------LLEALRAAAELAAQLEELEE-----AEEALLERLERLEEELEELEEALA-ELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 509 LLRAEDGILEngTDAHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAE-KIEDELKAEKRK 587
Cdd:COG1196 440 EEEALEEAAE--EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALLLA 517
|
330
....*....|
gi 1039727776 588 LQRELRSALD 597
Cdd:COG1196 518 GLRGLAGAVA 527
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
351-582 |
2.96e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 351 EVKEALRQREeMLEEIRQLQQKQAGFIREISDLQETIEWkdkkiGALERQKEFFDSIRSERDDLREETVKLKEELKKHgi 430
Cdd:COG4913 243 ALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAA-----LRLWFAQRRLELLEAELEELRAELARLEAELERL-- 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 431 ilnseiatngetsdtvndvgyQAPTKITKEELNALK----SAGEGTLDvRLKKLIDERECLLEQIKKLKGQLEGRQKNNK 506
Cdd:COG4913 315 ---------------------EARLDALREELDELEaqirGNGGDRLE-QLEREIERLERELEERERRRARLEALLAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 507 LDLLRAEDGILENGTDAH------------VMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSA-AEN 573
Cdd:COG4913 373 LPLPASAEEFAALRAEAAallealeeeleaLEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAlAEA 452
|
....*....
gi 1039727776 574 AEKIEDELK 582
Cdd:COG4913 453 LGLDEAELP 461
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
267-618 |
4.06e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 4.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 267 DTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEqlaeSQRQYEEKNKEFEREKHAHSILQ 346
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE----LEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 347 FQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWK---DKKIGALERQKEFFDSIRSERDDLREETVKLKE 423
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELreiEKRLSRLEEEINGIEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 424 ELKKhgiiLNSEIATNGETSDTVNDVgyqaptKITKEELNALKSAGEGTLDVRLKKLIDE----RECLLEQIKKL---KG 496
Cdd:PRK03918 346 KLKE----LEKRLEELEERHELYEEA------KAKKEELERLKKRLTGLTPEKLEKELEElekaKEEIEEEISKItarIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 497 QLEGRQKNNKLDL--LRAEDGIL----ENGTDAHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLE------SQV 564
Cdd:PRK03918 416 ELKKEIKELKKAIeeLKKAKGKCpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEkvlkkeSEL 495
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1039727776 565 TRYRSAAENAEKIEDELKA----EKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 618
Cdd:PRK03918 496 IKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
266-621 |
4.11e-04 |
|
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: 43.81 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 266 MDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLEleeqlaeSQRQYEEKNKEFEREKHAHSIL 345
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKK-------ALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 346 QFQFAEVKEALRQREEMLEEIRQLQQKQagfirEISDLQETIEWKDKKIGALERQKEFFDSIRSERDDLREEtVKLKEEL 425
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQ-----EIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEE-LKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 426 KKHGIILNSEIATNGETSDTVNDVGYQAPTKITKEELNALKSAGEGTLdvRLKKLIDERECLLEQIKKLKGQLEGRQKNN 505
Cdd:pfam02463 305 LERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKRE--AEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 506 KLDLLRAEDGILENGTDAHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEK 585
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLK 462
|
330 340 350
....*....|....*....|....*....|....*.
gi 1039727776 586 RKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRS 621
Cdd:pfam02463 463 DELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
350-623 |
4.38e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 350 AEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEW----------------KDKKIGALERQKEFFDSIRSERDD 413
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgreltEEHRKELLEEYTAELKRIEKELKE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 414 LREETVKLKEELKKHGIILN--SEIATNGETSDTVNDVgYQAPTKITKEELNALKSAGEGTLDvRLKKLIDERECLLEQI 491
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKkeSELIKLKELAEQLKEL-EEKLKKYNLEELEKKAEEYEKLKE-KLIKLKGEIKSLKKEL 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 492 KKLKGqLEGRQK--NNKLDLLRAE----DGILENGTDAHVMDLQ----------------RDANRQISDLKFKLAKSEQE 549
Cdd:PRK03918 549 EKLEE-LKKKLAelEKKLDELEEElaelLKELEELGFESVEELEerlkelepfyneylelKDAEKELEREEKELKKLEEE 627
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039727776 550 ITALEQNVIRLESQVTRYRSAAENAEKIEDE-----LKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSAL 623
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
329-436 |
6.95e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 329 EEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRqlqqkqagfiREISDLQETIEWKDKKIGALERQKEFFDSIR 408
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
|
90 100
....*....|....*....|....*...
gi 1039727776 409 SERDDLREETVKLKEELKKhgiiLNSEI 436
Cdd:COG2433 458 RREIRKDREISRLDREIER----LEREL 481
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
272-603 |
7.69e-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: 42.70 E-value: 7.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 272 IREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESQRQYEEKNKEFEREKHAHSILQFQFAE 351
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 352 VKEALRQREEmleEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIRSERDDLREEtvkLKEELKkhgiI 431
Cdd:TIGR04523 403 QEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES---LETQLK----V 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 432 LNSEIATNGETSDTVndvgyQAPTKITKEELNALKSAGEgTLDVRLKKLIDERECLLEQIKKLKgqLEGRQKNNKLDLLR 511
Cdd:TIGR04523 473 LSRSINKIKQNLEQK-----QKELKSKEKELKKLNEEKK-ELEEKVKDLTKKISSLKEKIEKLE--SEKKEKESKISDLE 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 512 AEDGILENGTDAHVMDLQRDANRQ--------ISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKA 583
Cdd:TIGR04523 545 DELNKDDFELKKENLEKEIDEKNKeieelkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
330 340
....*....|....*....|
gi 1039727776 584 EKRKLQRELRSALDKTEELE 603
Cdd:TIGR04523 625 ENEKLSSIIKNIKSKKNKLK 644
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
269-620 |
8.18e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 8.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 269 EASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLE--------LEEQLAESQRQYEEKNKEFEREKh 340
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRKELLEEYTAELKRIEKEL- 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 341 ahsilqfqfAEVKEALRQREEMLEEIRQLQQKQAGFI--REISDLQETIEWKDKKIGA--LERQKEFFDSIRSERDDLRE 416
Cdd:PRK03918 469 ---------KEIEEKERKLRKELRELEKVLKKESELIklKELAEQLKELEEKLKKYNLeeLEKKAEEYEKLKEKLIKLKG 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 417 ETVKLKEELKKhGIILNSEIATNGETSDTVNdvgyqaptKITKEELNALKSAGEGT---LDVRLKKL--IDERECLLEQI 491
Cdd:PRK03918 540 EIKSLKKELEK-LEELKKKLAELEKKLDELE--------EELAELLKELEELGFESveeLEERLKELepFYNEYLELKDA 610
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 492 KKLKGQLEGRQKNNKLDLLRAEDGILENGTDAhvmdlqRDANRQISDLKFKLakSEQEITALEQNVIRLESQVTRYRSAA 571
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETEKRL------EELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAEL 682
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1039727776 572 ENAEKIEDELKAEKRKLQRELRSALDKTEELEVsnghLVKRLEKMKANR 620
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
472-601 |
8.61e-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: 41.45 E-value: 8.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 472 TLDVRLKKLIDERECLLEQIKKLKGQLEGRQK-----NNKLDLLRAEDGILENGTDAHVMDLQRD--------ANRQISD 538
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEArleaaKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrNNKEYEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039727776 539 LKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 601
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
378-623 |
9.41e-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: 42.06 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 378 REISDLQETIEWKDKKIGALERQKEffdSIRSERDDLREETVKLKEELKKhgiilnseiatngetsdtvndvgyqaptki 457
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEK---ALLKQLAALERRIAALARRIRA------------------------------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 458 TKEELNALKSagegtldvRLKKLIDERECLLEQIKKLKGQLEGR----QKNNKLDLLRaedgILENGTDAhvmdlqRDAN 533
Cdd:COG4942 74 LEQELAALEA--------ELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPLA----LLLSPEDF------LDAV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 534 RQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRL 613
Cdd:COG4942 136 RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
250
....*....|
gi 1039727776 614 EKMKANRSAL 623
Cdd:COG4942 216 AELQQEAEEL 225
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
329-519 |
1.91e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 329 EEKNKEFEREKHAHSILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIR 408
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 409 sERDDLREETVKLKEELKKhgiiLNSEIATNGETSDTVNDVGYQAptKITKEELNALKSAGEGTLDVRLKKLIDERECLL 488
Cdd:COG4717 133 -ELEALEAELAELPERLEE----LEERLEELRELEEELEELEAEL--AELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|.
gi 1039727776 489 EQIKKLKGQLEgrQKNNKLDLLRAEDGILEN 519
Cdd:COG4717 206 QRLAELEEELE--EAQEELEELEEELEQLEN 234
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
353-627 |
1.98e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.58 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 353 KEALRQREEMLEEIRQLQQKQAgfireISDLQETIEWKDKKIGALERQKEFFDSIrserDDLREETVKLKEELKKHgiil 432
Cdd:PRK10929 25 EKQITQELEQAKAAKTPAQAEI-----VEALQSALNWLEERKGSLERAKQYQQVI----DNFPKLSAELRQQLNNE---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 433 nseiatngetSDTVNDVgyqaPTKITKEELNalksagEGTLDVRLKKLIDERECLLEQ-----IKKLKGQLEGRQKNNKL 507
Cdd:PRK10929 92 ----------RDEPRSV----PPNMSTDALE------QEILQVSSQLLEKSRQAQQEQdrareISDSLSQLPQQQTEARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 508 DLLRAEDGILENGTDAHVMDLQRDANRQISDLKFKLAKSEQEITAL----EQNVIRLESQVTRYRSaaenaEKIEDELKA 583
Cdd:PRK10929 152 QLNEIERRLQTLGTPNTPLAQAQLTALQAESAALKALVDELELAQLsannRQELARLRSELAKKRS-----QQLDAYLQA 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1039727776 584 EKRKL----QRELRSALDKTEELEVSNGHLVKRL-EKMKANR--SALLSQQ 627
Cdd:PRK10929 227 LRNQLnsqrQREAERALESTELLAEQSGDLPKSIvAQFKINRelSQALNQQ 277
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
345-617 |
3.94e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 345 LQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFFDSIRSERDDLREETVKLKEE 424
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 425 LKKHGIILnseiatnGETSDTVNDVgyQAPTKITKEELNALKS-AGEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQK 503
Cdd:PRK03918 254 KRKLEEKI-------RELEERIEEL--KKEIEELEEKVKELKElKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 504 NNKLDLLRAEdgilengtdahvmdlqrDANRQISDLKFKLAKSEQEITALE------QNVIRLESQVTRYRS--AAENAE 575
Cdd:PRK03918 325 GIEERIKELE-----------------EKEERLEELKKKLKELEKRLEELEerhelyEEAKAKKEELERLKKrlTGLTPE 387
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1039727776 576 KIEDELK-AEKRK--LQRELRSALDKTEELEVSNGHLVKRLEKMK 617
Cdd:PRK03918 388 KLEKELEeLEKAKeeIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
343-519 |
3.98e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 343 SILQFQFAEVKEALRQREEMLEEIRQLQQKQAGFIREISDLQ--ETIEWKDKKIGALER--------QKEFFDSIRSERD 412
Cdd:PRK05771 86 ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwGNFDLDLSLLLGFKYvsvfvgtvPEDKLEELKLESD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 413 DLREETVKLKEE--------LKKHGIILNSEIATNGETSDTVNDVGyqaptkITKEELNALKSagegtldvRLKKLIDER 484
Cdd:PRK05771 166 VENVEYISTDKGyvyvvvvvLKELSDEVEEELKKLGFERLELEEEG------TPSELIREIKE--------ELEEIEKER 231
|
170 180 190
....*....|....*....|....*....|....*
gi 1039727776 485 ECLLEQIKKLKGQLEgrqknnklDLLRAEDGILEN 519
Cdd:PRK05771 232 ESLLEELKELAKKYL--------EELLALYEYLEI 258
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
323-576 |
4.47e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 323 ESQRQYEEKNKEFEREKhahsilqfqfaevkealRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKE 402
Cdd:COG4942 31 QLQQEIAELEKELAALK-----------------KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 403 ffdSIRSERDDLREETVKLKEELKKHGIILNSEIATNGET-SDTVNDVGY-QAPTKITKEELNALKSAGEgtldvRLKKL 480
Cdd:COG4942 94 ---ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDfLDAVRRLQYlKYLAPARREQAEELRADLA-----ELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 481 IDERECLLEQIKKLKGQLEGRQKnnKLDLLRAEdgilengtdahvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRL 560
Cdd:COG4942 166 RAELEAERAELEALLAELEEERA--ALEALKAE------------------RQKLLARLEKELAELAAELAELQQEAEEL 225
|
250
....*....|....*.
gi 1039727776 561 ESQVTRYRSAAENAEK 576
Cdd:COG4942 226 EALIARLEAEAAAAAE 241
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
327-618 |
5.15e-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: 40.04 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 327 QYEEKNKEFEREKHAHSILQFQFAEvkealRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEffdS 406
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEELR-----EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE---E 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 407 IRSERDDLREETVKLKEELKkhgiilnseiatngetsdtvndvgyqaptkITKEELNALKSAGEgTLDVRLKKLIDEREC 486
Cdd:TIGR02168 286 LQKELYALANEISRLEQQKQ------------------------------ILRERLANLERQLE-ELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 487 LLEQIKKLKGQLEGRQKN-----NKLDLLRAEDGILENGtdahvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLE 561
Cdd:TIGR02168 335 LAEELAELEEKLEELKEElesleAELEELEAELEELESR--------LEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039727776 562 SQVT-----RYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 618
Cdd:TIGR02168 407 ARLErledrRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
463-627 |
9.04e-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: 39.27 E-value: 9.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 463 NALKSAGEGTLDVRLKKLIDERECLLEQIKKLKGQLEG--RQKNN---KLDLLRAEDGILENGTDAHVMDL------QRD 531
Cdd:TIGR02168 220 AELRELELALLVLRLEELREELEELQEELKEAEEELEEltAELQEleeKLEELRLEVSELEEEIEELQKELyalaneISR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 532 ANRQISDLKFKLAKSEQEITALEQNVIRLESQVTRYRSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVK 611
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
170
....*....|....*.
gi 1039727776 612 RLEKMKANRSALLSQQ 627
Cdd:TIGR02168 380 QLETLRSKVAQLELQI 395
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
355-553 |
9.53e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 9.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 355 ALRQREEMLEEIRQLQQKQAGFIREISDLQETIEWKDKKIGALERQKEFF------DSIRSERDDLREETVKLKEElkkh 428
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDAS---- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039727776 429 giilNSEIATNGETSDTVndvgyqaptkitKEELNALKSAgEGTLDVRLKKLIDERECLLEQIKKLKGQLEGRQKNNKLD 508
Cdd:COG4913 684 ----SDDLAALEEQLEEL------------EAELEELEEE-LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1039727776 509 L-LRAEDGILENGTDAHVMDLQRDANRQISDLKFKLAKSEQEITAL 553
Cdd:COG4913 747 LrALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| |
