|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
212-565 |
4.58e-85 |
|
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: 268.87 E-value: 4.58e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 212 VEDRPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKelnelkdqiqdvegkym 282
Cdd:pfam09738 30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 283 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQF 362
Cdd:pfam09738 93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 363 AEVKEALKEREEMLEeirqlqqkqassireisdlqetiewkdkkigalerqkeffdsvrserddlreevvmlkeelkKHG 442
Cdd:pfam09738 166 AELKEQLKQRDELIE--------------------------------------------------------------KHG 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 443 IILNSEIATNGEtsdTLNNVGYQGPTKMTKAELNALKSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQ--KIGKL 520
Cdd:pfam09738 184 LVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTR 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 966979245 521 DNLRSEDDVLENGTdmHVMDLQRDANRQISDLKFKLAKSEQEITA 565
Cdd:pfam09738 261 SSQSPDGFGLENGS--HVIEVQREANKQISDYKFKLQKAEQEITT 303
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
262-615 |
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: 57.76 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 262 REIKELNELkdqiqdvegkymqgLKEMKDSLAEVEEKYKKAMVSNAQLDNEktnfmyqVDTLKDMLLELEEQLAESRRQY 341
Cdd:TIGR02168 677 REIEELEEK--------------IEELEEKIAELEKALAELRKELEELEEE-------LEQLRKELEELSRQISALRKDL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 342 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEirqLQQKQASSIREISDLQETIewkdkkigalERQKEFFDSVR 421
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE---AEEELAEAEAEIEELEAQI----------EQLKEELKALR 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 422 SERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVGYQgpTKMTKAELNALKSTGDgTLDIRLKKLVDERECLL 501
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ--IEELSEDIESLAAEIE-ELEELIEELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 502 EQIKKLKGQLEERQKigKLDNLRSEDDVLENGtdmhvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVS-RY 580
Cdd:TIGR02168 880 NERASLEEALALLRS--ELEELSEELRELESK--------RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEY 949
|
330 340 350
....*....|....*....|....*....|....*
gi 966979245 581 KSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 615
Cdd:TIGR02168 950 SLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
361-639 |
3.86e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 361 QFAEVKEALK-EREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGAL----ERQKEFFDSVRSERDDLREEVVMLK 435
Cdd:TIGR02169 678 RLRERLEGLKrELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeeEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 436 EELKKhgiiLNSEIAtngETSDTLNNVgyqgptkmtKAELNALKstgDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQ 515
Cdd:TIGR02169 758 SELKE----LEARIE---ELEEDLHKL---------EEALNDLE---ARLSHSRIPEIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 516 KigKLDNLRSEDDVLEngtdmhvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELK 595
Cdd:TIGR02169 819 Q--KLNRLTLEKEYLE--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 966979245 596 AEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQ 639
Cdd:TIGR02169 889 KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
363-639 |
9.09e-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: 9.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 363 AEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKHG 442
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 443 IILNSEIATNGETSDTLNNvgyqgptkmtkaELNALKSTGD------GTLDIRLKKLVDERECLLEQIKKLKGQLEERQK 516
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKE------------ELKALREALDelraelTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 517 IGKldnlRSEDDVLEngtdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKA 596
Cdd:TIGR02168 846 QIE----ELSEDIES-------------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 966979245 597 EKRKLQRELrsaldktEELEVSNGHLVKRLEKMKANRSALLSQ 639
Cdd:TIGR02168 909 KRSELRREL-------EELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
309-616 |
4.37e-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: 53.15 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 309 LDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQAS 388
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 389 sirEISDLQETIEWKDKKIGALERQ--KEFFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNN-VGYQ 465
Cdd:TIGR02169 766 ---RIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElQEQR 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 466 GPTKMTKAELNA---LKSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGTDmhvmdlq 542
Cdd:TIGR02169 843 IDLKEQIKSIEKeieNLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA--QLRELERKIEELEAQIE------- 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 543 rDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSA---AENAEKIE------------------------DELK 595
Cdd:TIGR02169 914 -KKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLedvQAELQRVEeeiralepvnmlaiqeyeevlkrlDELK 992
|
330 340
....*....|....*....|.
gi 966979245 596 AEKRKLQRELRSALDKTEELE 616
Cdd:TIGR02169 993 EKRAKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
363-637 |
1.02e-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: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 363 AEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWK-------DKKIGALERQK----------------EFFDS 419
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVkselkelEARIEELEEDLhkleealndlearlshSRIPE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 420 VRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNN-VGYQGPTKMTKAELNA---LKSTGDGTLDIRLKKLVD 495
Cdd:TIGR02169 796 IQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQElQEQRIDLKEQIKSIEKeieNLNGKKEELEEELEELEA 875
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 496 ERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGTDmhvmdlqrDANRQISDLKFKLAKSEQEITALEQNVIRLES 575
Cdd:TIGR02169 876 ALRDLESRLGDLKKERDELEA--QLRELERKIEELEAQIE--------KKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966979245 576 QVSryksaaenAEKIEDELKAEKRKLQRELRS-------ALDKTEELEVSNGHLVKRLEKMKANRSALL 637
Cdd:TIGR02169 946 IPE--------EELSLEDVQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
338-615 |
1.39e-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: 51.60 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 338 RRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----KEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQ 413
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 414 KE----FFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGEtsdtlnnvgyqgptkmTKAELNALKSTGDgTLDIR 489
Cdd:TIGR02168 318 LEeleaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE----------------LEAELEELESRLE-ELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 490 LKKLVDERECLLEQIKKLKGQ---LEERQKIGKLDNLRSEDDVLENGTDMHVMDLQrDANRQISDLKFKLAKSEQEITAL 566
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELEEELEELQEELERL 459
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 966979245 567 EQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 615
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
265-639 |
2.37e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.79 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 265 KELNELKDQIQDVEGKYMQGL-KEMKDSLAEVEEKYKkamvsnaQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEE 343
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQKEQDWnKELKSELKNQEKKLE-------EIQNQISQNNKIISQLNEQISQLKKELTNSESENSE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 344 KNKEFErEKHAhsilqfqfaEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSE 423
Cdd:TIGR04523 361 KQRELE-EKQN---------EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE---LLEKE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 424 RDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQGPTKM--TKAELNALKSTGDgtldiRLKKLVDERECLL 501
Cdd:TIGR04523 428 IERLKETIIKNNSEIKD----LTNQDSVKELIIKNLDNTRESLETQLkvLSRSINKIKQNLE-----QKQKELKSKEKEL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 502 EQIKKLKGQLEERQK---------IGKLDNLRSEDDVLENGTDmhvmDLQRDANRQISDLKFKLAksEQEITALEQNVIR 572
Cdd:TIGR04523 499 KKLNEEKKELEEKVKdltkkisslKEKIEKLESEKKEKESKIS----DLEDELNKDDFELKKENL--EKEIDEKNKEIEE 572
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966979245 573 LESQVSRYKSAAENAEKIEDELKAEKRKLQRELrsaldktEELEVSNGHLVKRLEKMKANRSALLSQ 639
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSI 632
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
256-596 |
7.50e-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: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 256 DTEASIREI-KELNELKDQIQDVEgkymqglKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVdtlKDMLLELEEQL 334
Cdd:TIGR02169 234 ALERQKEAIeRQLASLEEELEKLT-------EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV---KEKIGELEAEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 335 AESRRQYEEKNKEFERekhAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQk 414
Cdd:TIGR02169 304 ASLERSIAEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 415 efFDSVRSERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQgptkmTKAELNALKStgdgtldiRLKKLV 494
Cdd:TIGR02169 380 --FAETRDELKDYREKLEKLKREINE----LKRELDRLQEELQRLSEELAD-----LNAAIAGIEA--------KINELE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 495 DERECLLEQIKKLKGQLEERQKIGKldnlrseddvlengtdmhvmdlqrDANRQISDLKFKLAKSEQEITALEQNVIRLE 574
Cdd:TIGR02169 441 EEKEDKALEIKKQEWKLEQLAADLS------------------------KYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
330 340
....*....|....*....|..
gi 966979245 575 SQVSRYKSAAENAEKIEDELKA 596
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEVLKA 518
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
363-589 |
9.41e-06 |
|
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: 48.22 E-value: 9.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 363 AEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVMLKEELKKHG 442
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA---ELRAELEAQKEELAELLRALYRLG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 443 IILNSEIATNGETSDTLNNVG--YQGPTKMTKAELNALKSTGDgtldiRLKKLVDERECLLEQIKKLKGQLEERQKigKL 520
Cdd:COG4942 118 RQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLA-----ELAALRAELEAERAELEALLAELEEERA--AL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966979245 521 DNLRSEddvlengtdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEK 589
Cdd:COG4942 191 EALKAE------------------RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
280-640 |
2.07e-05 |
|
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: 47.71 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 280 KYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQ 359
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 360 FQFAEVKEAL------KEREEMLEEIRQLQQKQassiREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVM 433
Cdd:TIGR04523 288 KQLNQLKSEIsdlnnqKEQDWNKELKSELKNQE----KKLEEIQNQISQNNKIISQLNEQIS---QLKKELTNSESENSE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 434 LKEELKKHGIILNSEIATNGETSDTLNNVgyqgptkmtKAELNALKSTGDGT------LDIRLKKLVDERECLLEQIKKL 507
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNL---------ESQINDLESKIQNQeklnqqKDEQIKKLQQEKELLEKEIERL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 508 KGQLEERQKigKLDNLRSEDDVLENGTDMH----------VMDLQRDANRQISDLKFK---LAKSEQEITALEQNVIRLE 574
Cdd:TIGR04523 432 KETIIKNNS--EIKDLTNQDSVKELIIKNLdntresletqLKVLSRSINKIKQNLEQKqkeLKSKEKELKKLNEEKKELE 509
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966979245 575 SQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALD---------KTEELEVSNGHLVKRLEKMKANRSALLSQQ 640
Cdd:TIGR04523 510 EKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelnkddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQ 584
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
361-640 |
2.69e-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: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 361 QFAEVKEALKERE--EMLEEIRQLQQKQASSIREISDLQETIE----WKDKKIGALERQKEFFDSVRSERDDLREEVVML 434
Cdd:COG1196 214 RYRELKEELKELEaeLLLLKLRELEAELEELEAELEELEAELEeleaELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 435 KEELKKHGIILNSEIATNGETSDTLNNVGYQgpTKMTKAELNALKSTGDgTLDIRLKKLVDERECLLEQIKKLKGQLEER 514
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEELEEE--LAELEEELEELEEELE-ELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 515 QKIgKLDNLRSEDDVLENgtDMHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDEL 594
Cdd:COG1196 371 EAE-LAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 966979245 595 KAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 640
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
261-633 |
3.07e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 261 IREIKELNELKDQIQDVEGKymqgLKEMKDSLAEVEEK---YKKAMVSNAQLDNEKTNFM-YQVDTLKDMLLELEEQLAE 336
Cdd:PRK03918 327 EERIKELEEKEERLEELKKK----LKELEKRLEELEERhelYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKAKEE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 337 SRRQYEE--------KNKEFEREK----------------------HAHSILQFQFAEVKEALKEREEMLEEIRQL---- 382
Cdd:PRK03918 403 IEEEISKitarigelKKEIKELKKaieelkkakgkcpvcgrelteeHRKELLEEYTAELKRIEKELKEIEEKERKLrkel 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 383 --------QQKQASSIREISDLQETIEWKDKKIGA--LERQKEFFDSVRSERDDLREEVVMLKEELKKhGIILNSEIATN 452
Cdd:PRK03918 483 relekvlkKESELIKLKELAEQLKELEEKLKKYNLeeLEKKAEEYEKLKEKLIKLKGEIKSLKKELEK-LEELKKKLAEL 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 453 GETSDTLnnvgyqgptKMTKAELNA-LKSTGDGTLD----------------IRLKKLVDERECLLEQIKKLKGQLEErq 515
Cdd:PRK03918 562 EKKLDEL---------EEELAELLKeLEELGFESVEeleerlkelepfyneyLELKDAEKELEREEKELKKLEEELDK-- 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 516 kigKLDNLRSEDDVLEngtdmhvmdlqrDANRQISDLKFKLakSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELK 595
Cdd:PRK03918 631 ---AFEELAETEKRLE------------ELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAELEELEKRREEIK 693
|
410 420 430
....*....|....*....|....*....|....*...
gi 966979245 596 AEKRKLQRELRSALDKTEELEVsnghLVKRLEKMKANR 633
Cdd:PRK03918 694 KTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
363-616 |
3.67e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 363 AEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETiewKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKHG 442
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEK---RDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 443 IILNSEIATNGETSDTLNNVGYQGPTKMT-KAELNALKSTGDgTLDIRLKKlvdEREcLLEQIKKLKGQLEERQKI---- 517
Cdd:COG1340 85 EKLNELREELDELRKELAELNKAGGSIDKlRKEIERLEWRQQ-TEVLSPEE---EKE-LVEKIKELEKELEKAKKAlekn 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 518 GKLDNLRSEDDVLENGTDMHVMDLQRDANrQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAE 597
Cdd:COG1340 160 EKLKELRAELKELRKEAEEIHKKIKELAE-EAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
250
....*....|....*....
gi 966979245 598 KRKLQRELRSALDKTEELE 616
Cdd:COG1340 239 LRELRKELKKLRKKQRALK 257
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
340-631 |
5.21e-05 |
|
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: 46.59 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 340 QYEEKNKEFEREKHAHSILQFQFAEvkealKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALER-----QK 414
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEELR-----EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEeieelQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 415 EFFdSVRSERDDLREEVVMLKEELKKhgiiLNSEIatngetsdtlnnvgyqgptKMTKAELNALKSTGDgtldiRLKKLV 494
Cdd:TIGR02168 289 ELY-ALANEISRLEQQKQILRERLAN----LERQL-------------------EELEAQLEELESKLD-----ELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 495 DERECLLEQIKKLKGQLEErqkigKLDNLRSEDDVLENGtdmhvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLE 574
Cdd:TIGR02168 340 AELEEKLEELKEELESLEA-----ELEELEAELEELESR--------LEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966979245 575 SQVSRYKSAAENA-EKIEDELK----AEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 631
Cdd:TIGR02168 407 ARLERLEDRRERLqQEIEELLKkleeAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
342-459 |
7.15e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.00 E-value: 7.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 342 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 421
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
|
90 100 110
....*....|....*....|....*....|....*...
gi 966979245 422 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 459
Cdd:COG2433 458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
367-603 |
9.38e-05 |
|
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: 45.83 E-value: 9.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 367 EALKEREEMLE---EIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFD----SVRSERDDLREEVVMLKEELK 439
Cdd:TIGR02169 288 EQLRVKEKIGEleaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEreieEERKRRDKLTEEYAELKEELE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 440 KHGIILNSEIATNGETSDTLnnVGYQGPTKMTKAELNALKSTGDGTLDiRLKKLVDERECLLEQIKKLKGQLEERqkigk 519
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDEL--KDYREKLEKLKREINELKRELDRLQE-ELQRLSEELADLNAAIAGIEAKINEL----- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 520 ldnlrseDDVLEngtdmhvmdlqrdanrqisDLKFKLAKSEQEITALEQNVIRLESQVSRYKsaaENAEKIEDELKAEKR 599
Cdd:TIGR02169 440 -------EEEKE-------------------DKALEIKKQEWKLEQLAADLSKYEQELYDLK---EEYDRVEKELSKLQR 490
|
....
gi 966979245 600 KLQR 603
Cdd:TIGR02169 491 ELAE 494
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
353-608 |
1.03e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 353 HAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERqkeffdsvrsERDDLREEVV 432
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----------EIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 433 MLKEELKKhgiiLNSEIATNGETSDTLNNVgyqgptkmtkaeLNAlKSTGD--GTLDIrLKKLVDERECLLEQIKKLKGQ 510
Cdd:COG3883 83 ERREELGE----RARALYRSGGSVSYLDVL------------LGS-ESFSDflDRLSA-LSKIADADADLLEELKADKAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 511 LEERQKigKLDNLRSEddvlengtdmhVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKI 590
Cdd:COG3883 145 LEAKKA--ELEAKLAE-----------LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
250
....*....|....*...
gi 966979245 591 EDELKAEKRKLQRELRSA 608
Cdd:COG3883 212 AAAAAAAAAAAAAAAAAA 229
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
342-532 |
1.09e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 342 EEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVR 421
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 422 sERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQGptKMTKAELNALKSTGDGTLDIRLKKLVDERECLL 501
Cdd:COG4717 133 -ELEALEAELAELPERLEE----LEERLEELRELEEELEELEAEL--AELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|.
gi 966979245 502 EQIKKLKGQLEERQKigKLDNLRSEDDVLEN 532
Cdd:COG4717 206 QRLAELEEELEEAQE--ELEELEEELEQLEN 234
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
383-636 |
1.45e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 383 QQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVMLKEELKKhgiilnseiatngetsdtlnnv 462
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEK---ALLKQLAALERRIAALARRIRA---------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 463 gyqgptkmTKAELNALKStgdgtldiRLKKLVDERECLLEQIKKLKGQLEER----QKIGKLDNLrsedDVLENGTDMhv 538
Cdd:COG4942 74 --------LEQELAALEA--------ELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPL----ALLLSPEDF-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 539 mdlqRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVS 618
Cdd:COG4942 132 ----LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
250
....*....|....*...
gi 966979245 619 NGHLVKRLEKMKANRSAL 636
Cdd:COG4942 208 LAELAAELAELQQEAEEL 225
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
347-636 |
1.90e-04 |
|
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: 44.67 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 347 EFEREKHAhsiLQFQFAEVKEALKEREEMLEEIRQLQQK------QASSIREISDLQETIEWKD--KKIGALERQKEffd 418
Cdd:TIGR02169 167 EFDRKKEK---ALEELEEVEENIERLDLIIDEKRQQLERlrrereKAERYQALLKEKREYEGYEllKEKEALERQKE--- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 419 SVRSERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLN------NVGYQGPTKMTKAELNALKSTGDGT------- 485
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISE----LEKRLEEIEQLLEELNkkikdlGEEEQLRVKEKIGELEAEIASLERSiaekere 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 486 ---LDIRLKKLVDERECLLEQIKKLKGQLEERQK-----IGKLDNLRSEDDVLEN------GTDMHVMDLQRDANRQISD 551
Cdd:TIGR02169 317 ledAEERLAKLEAEIDKLLAEIEELEREIEEERKrrdklTEEYAELKEELEDLRAeleevdKEFAETRDELKDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 552 LKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 631
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKE 476
|
....*
gi 966979245 632 NRSAL 636
Cdd:TIGR02169 477 EYDRV 481
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
361-631 |
2.34e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 361 QFAEVKEA------LKEREEMLEEIRQLQQKQASSIREISDLQETIEWkdkkiGALERQKEFFDSVRSERDDLREEVVML 434
Cdd:COG4913 233 HFDDLERAhealedAREQIELLEPIRELAERYAAARERLAELEYLRAA-----LRLWFAQRRLELLEAELEELRAELARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 435 KEELKkhgiilnseiatngetsdtlnnvgyqgptkmtkaelnalkstgdgTLDIRLKKLVDERECLLEQIKKLKGQleer 514
Cdd:COG4913 308 EAELE---------------------------------------------RLEARLDALREELDELEAQIRGNGGD---- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 515 qkigKLDNLRSEDDVLENGTDmHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAekiEDEL 594
Cdd:COG4913 339 ----RLEQLEREIERLERELE-ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA---LAEA 410
|
250 260 270
....*....|....*....|....*....|....*..
gi 966979245 595 KAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 631
Cdd:COG4913 411 EAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
338-639 |
5.51e-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: 43.18 E-value: 5.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 338 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKI--GALERQKE 415
Cdd:pfam15921 568 RQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnAGSERLRA 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 416 FFDsVRSERDDLREEVvmlkeelkkhgiilnseiatngetsdtlnnvgyqgptKMTKAELNALKSTgdgtLDIRLKKLVD 495
Cdd:pfam15921 648 VKD-IKQERDQLLNEV-------------------------------------KTSRNELNSLSED----YEVLKRNFRN 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 496 ERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLEnGTDMHVMDLQRDANRQIsdlkfklakseqeiTALEQNVIRLES 575
Cdd:pfam15921 686 KSEEMETTTNKLKMQLKSAQS--ELEQTRNTLKSME-GSDGHAMKVAMGMQKQI--------------TAKRGQIDALQS 748
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 966979245 576 QVSRYKSAAENAEKIEDELKAEKRKLQRELRS-ALDKTE---ELEVSNGHlVKRLEKMKANRSALLSQ 639
Cdd:pfam15921 749 KIQFLEEAMTNANKEKHFLKEEKNKLSQELSTvATEKNKmagELEVLRSQ-ERRLKEKVANMEVALDK 815
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
263-636 |
6.97e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 263 EIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFmyqVDTLKDMLLELEEQLAESRRQYE 342
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKL---KELEKRLEELEERHELYEEAKAK 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 343 EKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEW----------------KDKK 406
Cdd:PRK03918 371 KEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgreltEEHR 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 407 IGALERQKEFFDSVRSERDDLREEVVMLKEELKKHGIILN--SEIATNGETSDTLNNV-----GYQGPT--------KMT 471
Cdd:PRK03918 451 KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeSELIKLKELAEQLKELeeklkKYNLEElekkaeeyEKL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 472 KAELNALKSTGDGTLD--IRLKKLVDERECLLEQIKKLKGQLEERQKIGKLDNLRSEDDVLENGTDMHVMDLQ----RDA 545
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylelKDA 610
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 546 NRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDE-----LKAEKRKLQRELRSALDKTEELEVSNG 620
Cdd:PRK03918 611 EKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRRE 690
|
410
....*....|....*.
gi 966979245 621 HLVKRLEKMKANRSAL 636
Cdd:PRK03918 691 EIKKTLEKLKEELEER 706
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
471-636 |
7.14e-04 |
|
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: 42.74 E-value: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 471 TKAELNALKSTgdgtLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKLDNLRSEDDVLENGTDMHVMDLQRDANRQIS 550
Cdd:TIGR02168 696 LEKALAELRKE----LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE 771
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 551 DLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMK 630
Cdd:TIGR02168 772 EAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS 851
|
....*.
gi 966979245 631 ANRSAL 636
Cdd:TIGR02168 852 EDIESL 857
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
236-429 |
1.09e-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: 42.35 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 236 LASLGGTSSRRGSGDTSISIDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTN 315
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 316 FMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEM-LEEIRQLQQKQASSIREIS 394
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEAR 971
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 966979245 395 DLQETIEWKDKKIGA--------LERQKEFFDSVRSERDDLRE 429
Cdd:TIGR02168 972 RRLKRLENKIKELGPvnlaaieeYEELKERYDFLTAQKEDLTE 1014
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
485-614 |
1.40e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 485 TLDIRLKKLVDERECLLEQIKKLKGQLEERQK-----IGKLDNLRSEDDVLENGTDMHVMDLQRD--------ANRQISD 551
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEArleaaKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrNNKEYEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966979245 552 LKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 614
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
489-640 |
2.30e-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: 41.20 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 489 RLKKLVDERECLLEQIKKLKGQLEE-----RQKIGKLDNLRSEDDVLEN------GTDMHVMDLQRDANRQISDLKFKLA 557
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEEltaelQELEEKLEELRLEVSELEEeieelqKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 558 KSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALL 637
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
...
gi 966979245 638 SQQ 640
Cdd:TIGR02168 393 LQI 395
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
308-630 |
2.31e-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: 41.26 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 308 QLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREkhahsiLQFQFAEVKEALKEREEMLEEI----RQLQ 383
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQ------LVLANSELTEARTERDQFSQESgnldDQLQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 384 QKQASSIREISDLQETIEwKDKKIGALERQKEF-FDSVRSERDDLREEVVMLKEELKKhgiiLNSEiaTNGETSDTLNNV 462
Cdd:pfam15921 381 KLLADLHKREKELSLEKE-QNKRLWDRDTGNSItIDHLRRELDDRNMEVQRLEALLKA----MKSE--CQGQMERQMAAI 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 463 GYQGPTKMTKAELNA-LKSTGDgtldiRLKKLVDE---RECLLEQ----IKKLKGQLEERQKIGKLDNlrSEDDVLENGT 534
Cdd:pfam15921 454 QGKNESLEKVSSLTAqLESTKE-----MLRKVVEEltaKKMTLESsertVSDLTASLQEKERAIEATN--AEITKLRSRV 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 535 DMHVMDLQ---------RDANRQISDLKFKLAKSEQEITALEQ---NVIRLESQVSRyKSAAENAEKIEDELKAEKRKLQ 602
Cdd:pfam15921 527 DLKLQELQhlknegdhlRNVQTECEALKLQMAEKDKVIEILRQqieNMTQLVGQHGR-TAGAMQVEKAQLEKEINDRRLE 605
|
330 340 350
....*....|....*....|....*....|...
gi 966979245 603 -RELRSALDKTE----ELEVSNGHLvkRLEKMK 630
Cdd:pfam15921 606 lQEFKILKDKKDakirELEARVSDL--ELEKVK 636
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
258-440 |
2.75e-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: 40.81 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 258 EASIREIKELNELKDQIQdvegkymQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 337
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 338 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREemlEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFF 417
Cdd:TIGR02168 343 EEKLEELKEELESLEAELEELEAELEELESRLEELE---EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
170 180 190
....*....|....*....|....*....|..
gi 966979245 418 DS---------VRSERDDLREEVVMLKEELKK 440
Cdd:TIGR02168 420 QQeieellkklEEAELKELQAELEELEEELEE 451
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
262-614 |
3.00e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 262 REIKELNELKDQIQDVEGKymqgLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES--RR 339
Cdd:PRK03918 228 KEVKELEELKEEIEELEKE----LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSefYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 340 QYEEKNKEFEREKhahSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEW---------------KD 404
Cdd:PRK03918 304 EYLDELREIEKRL---SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeeakakkeelerlkKR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 405 KKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQGP------TKMTKAELNAL 478
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE----LKKEIKELKKAIEELKKAKGKCPvcgrelTEEHRKELLEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 479 KSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKLDNLRSEDDVLENGTDMHVMDLQRDANRQISDLKFKLAK 558
Cdd:PRK03918 457 YTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK 536
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 966979245 559 SEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 614
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEE 592
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
338-616 |
3.81e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.49 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 338 RRQYEEKNKEFER-------EKHAHSILQFQ---FAEVKEALKEREEMLEEIRQLQQKqassiREISDL-QETIEWKDKK 406
Cdd:pfam17380 302 RQEKEEKAREVERrrkleeaEKARQAEMDRQaaiYAEQERMAMERERELERIRQEERK-----RELERIrQEEIAMEISR 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 407 IGALERqkeffdsVRSERDDLREEVVMLKEELKKHGIILNSEiatngetsdtlnnvgyQGPTKMTKAELNALKSTGDGTL 486
Cdd:pfam17380 377 MRELER-------LQMERQQKNERVRQELEAARKVKILEEER----------------QRKIQQQKVEMEQIRAEQEEAR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 487 DIRLKKLVDERECLLE-----------QIKKLKGQLEERQKIGKLDNLRSEDDVLENGTDMHVMDLQRDANRQI---SDL 552
Cdd:pfam17380 434 QREVRRLEEERAREMErvrleeqerqqQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAmieEER 513
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966979245 553 KFKLAKSEQEitaLEQNVIRLESQvsRYKSAAENAEKIEDElkaEKRKLQRELRSALDKTEELE 616
Cdd:pfam17380 514 KRKLLEKEME---ERQKAIYEEER--RREAEEERRKQQEME---ERRRIQEQMRKATEERSRLE 569
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
321-634 |
4.29e-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: 40.34 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 321 DTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSilQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETI 400
Cdd:pfam02463 208 KALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ--ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 401 EWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGEtsdtlnnvgyqgpTKMTKAELNALKS 480
Cdd:pfam02463 286 EELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE-------------LEKELKELEIKRE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 481 TGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKLDNlrseddvlENGTDMHVMDLQRDANRQISDLKFKLAKSE 560
Cdd:pfam02463 353 AEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE--------EELELKSEEEKEAQLLLELARQLEDLLKEE 424
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966979245 561 QEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRS 634
Cdd:pfam02463 425 KKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
361-440 |
4.72e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 39.67 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 361 QFAEVKEALKER--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 438
Cdd:PRK05431 10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89
|
..
gi 966979245 439 KK 440
Cdd:PRK05431 90 DE 91
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
338-637 |
5.48e-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: 40.03 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 338 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFF 417
Cdd:TIGR00606 195 RQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKAL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 418 DSVRSERDDLREEVVMLKEELKKhgiilnseiATNGETSDTLNNvgyQGPTKMTKAELNALKSTGDGTLDIRLKKLVDER 497
Cdd:TIGR00606 275 KSRKKQMEKDNSELELKMEKVFQ---------GTDEQLNDLYHN---HQRTVREKERELVDCQRELEKLNKERRLLNQEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 498 ECLLEQIKKLKGQLEERQ-KIGKLDNLRseddvLENGTDMHVMDLQRDA--NRQISD-LKFKLAKSEQEITALEQNVIRL 573
Cdd:TIGR00606 343 TELLVEQGRLQLQADRHQeHIRARDSLI-----QSLATRLELDGFERGPfsERQIKNfHTLVIERQEDEAKTAAQLCADL 417
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966979245 574 ESQVsryKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEvsngHLVKRLEKMKANRSALL 637
Cdd:TIGR00606 418 QSKE---RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELK----FVIKELQQLEGSSDRIL 474
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
581-640 |
7.67e-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: 38.37 E-value: 7.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 581 KSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 640
Cdd:pfam11932 27 AAAAQSQKKI-DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQI 85
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
260-606 |
8.03e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.39 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 260 SIREIKELNELKDQIQDVEgkymqglkemkdSLAEVEEKYKKAMVSNA-QLDNEKTNFMYQVDtlkdmlleleeqlaesr 338
Cdd:pfam01576 456 NIKLSKDVSSLESQLQDTQ------------ELLQEETRQKLNLSTRLrQLEDERNSLQEQLE----------------- 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 339 rQYEEKNKEFEREKhahSILQFQFAEVKealKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQK---- 414
Cdd:pfam01576 507 -EEEEAKRNVERQL---STLQAQLSDMK---KKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKnrlq 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 415 EFFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVGYQGPTKMTKAElnalkstgdgTLDIRLKKLV 494
Cdd:pfam01576 580 QELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRAL----------SLARALEEAL 649
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 495 DERECLLEQIKKLKGQLEerqkigklDNLRSEDDVlenGTDMHVMD-LQRDANRQISDLKFKLAKSEQEITALEQNVIRL 573
Cdd:pfam01576 650 EAKEELERTNKQLRAEME--------DLVSSKDDV---GKNVHELErSKRALEQQVEEMKTQLEELEDELQATEDAKLRL 718
|
330 340 350
....*....|....*....|....*....|....
gi 966979245 574 ESQVSRYKSAAENAEKIEDELKAEKRK-LQRELR 606
Cdd:pfam01576 719 EVNMQALKAQFERDLQARDEQGEEKRRqLVKQVR 752
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
358-630 |
9.76e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 358 LQFQFAEVKEALKEREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEE 437
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 438 LKKHGIILNSEIATNGETSDTLNNVgyqgptKMTKAELNALKstGDGTLDIRLKKLVDERECLLEQIKKLKGQLEER--- 514
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEEL------EEKVKELKELK--EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEing 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 515 --QKIGKLDNLRSEDDVLENgtdmhvmdLQRDANRQISDLKfKLAKSEQEITALEQNVIRLESQVSRYKsaAENAEKIED 592
Cdd:PRK03918 326 ieERIKELEEKEERLEELKK--------KLKELEKRLEELE-ERHELYEEAKAKKEELERLKKRLTGLT--PEKLEKELE 394
|
250 260 270
....*....|....*....|....*....|....*...
gi 966979245 593 ELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMK 630
Cdd:PRK03918 395 ELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
372-609 |
9.94e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 372 REEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKHGIILNSEiat 451
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966979245 452 ngetsdtlnnvgyqgptkmtkaelnalkstgdgTLDIRLKKLVDERECLLEQIKKLKGQLEE-RQKIGKLDNLRSEDDVL 530
Cdd:COG4717 129 ---------------------------------PLYQELEALEAELAELPERLEELEERLEElRELEEELEELEAELAEL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966979245 531 ENGTDMHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKiEDELKAEKRKLQRELRSAL 609
Cdd:COG4717 176 QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLL 253
|
|
| |
