|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
212-565 |
8.06e-87 |
|
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: 273.11 E-value: 8.06e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 212 VEERPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKelnelkdqiqdvegkym 282
Cdd:pfam09738 30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIK----------------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 283 qglkemkDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQF 362
Cdd:pfam09738 93 -------HELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 363 AEVKEALKQREEMLEeirqlqqkqassireisdlqetiewkdkkigalerqkeffdsvrserddlreevvmlkeelkKHG 442
Cdd:pfam09738 166 AELKEQLKQRDELIE--------------------------------------------------------------KHG 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 443 IILNSEIATNGEtsdTLNNVGYQGPTKMTKEELNALKSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQ--KIGKL 520
Cdd:pfam09738 184 LVIVPDENTNGE---EENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTR 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 212276078 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 |
1.28e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.14 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 262 REIKELNELkdqiqdvegkymqgLKEMKDSLAEVEEKYKKAMVSNAQLDNEktnfmyqVDTLKDMLLELEEQLAESRRQY 341
Cdd:TIGR02168 677 REIEELEEK--------------IEELEEKIAELEKALAELRKELEELEEE-------LEQLRKELEELSRQISALRKDL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 342 EEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEirqLQQKQASSIREISDLQETIewkdkkigalERQKEFFDSVR 421
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE---AEEELAEAEAEIEELEAQI----------EQLKEELKALR 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 422 SERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVGYQgpTKMTKEELNALKSTGDgTLDIRLKKLVDERECLL 501
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ--IEELSEDIESLAAEIE-ELEELIEELESELEALL 879
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 502 EQIKKLKGQLEERQKigKLDNLRSEDDVLENGtdmhvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVS-RY 580
Cdd:TIGR02168 880 NERASLEEALALLRS--ELEELSEELRELESK--------RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEY 949
|
330 340 350
....*....|....*....|....*....|....*
gi 212276078 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 |
4.35e-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: 4.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 361 QFAEVKEALK-QREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGAL----ERQKEFFDSVRSERDDLREEVVMLK 435
Cdd:TIGR02169 678 RLRERLEGLKrELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeeEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 436 EELKKhgiiLNSEIAtngETSDTLNNVgyqgptkmtKEELNALKstgDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQ 515
Cdd:TIGR02169 758 SELKE----LEARIE---ELEEDLHKL---------EEALNDLE---ARLSHSRIPEIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 516 KigKLDNLRSEDDVLEngtdmhvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELK 595
Cdd:TIGR02169 819 Q--KLNRLTLEKEYLE--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 212276078 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 |
5.04e-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: 56.22 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 363 AEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQkefFDSVRSERDDLREEVVMLKEELKKhg 442
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER---IAQLSKELTELEAEIEELEERLEE-- 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 443 iiLNSEIATNGETSDTLnnvgyQGPTKMTKEELNALKSTGD------GTLDIRLKKLVDERECLLEQIKKLKGQLEERQK 516
Cdd:TIGR02168 773 --AEEELAEAEAEIEEL-----EAQIEQLKEELKALREALDelraelTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 517 IGKldnlRSEDDVLEngtdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKA 596
Cdd:TIGR02168 846 QIE----ELSEDIES-------------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 212276078 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 |
4.45e-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: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 309 LDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQAS 388
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 389 sirEISDLQETIEWKDKKIGALERQ--KEFFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVgyQG 466
Cdd:TIGR02169 766 ---RIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL--QE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 467 PTKMTKEELNALKSTGDgTLDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGTDMHVMDLQRdAN 546
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIE-NLNGKKEELEEELEELEAALRDLESRLGDLKK--ERDELEAQLRELERKIEELEAQIEK-KR 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 547 RQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSA---AENAEKIE------------------------DELKAEKR 599
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLedvQAELQRVEeeiralepvnmlaiqeyeevlkrlDELKEKRA 996
|
330
....*....|....*..
gi 212276078 600 KLQRELRSALDKTEELE 616
Cdd:TIGR02169 997 KLEEERKAILERIEEYE 1013
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
363-637 |
1.00e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 363 AEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWK-------DKKIGALER-----QKEFFDSVRSERDDLREE 430
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVkselkelEARIEELEEdlhklEEALNDLEARLSHSRIPE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 431 VVMLKEELKK-HGIILNSEIATNGETSDTLNNVGYQGPTKMTKEELNALkstgdgtLDIRLKKLVDERECLLEQIKKLKG 509
Cdd:TIGR02169 796 IQAELSKLEEeVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID-------LKEQIKSIEKEIENLNGKKEELEE 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 510 QLEE-----RQKIGKLDNLRSEDDVLENgtDMHVM-DLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSA 583
Cdd:TIGR02169 869 ELEEleaalRDLESRLGDLKKERDELEA--QLRELeRKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 212276078 584 AENAEKIEDeLKAEKRKLQRELRS-------ALDKTEELEVSNGHLVKRLEKMKANRSALL 637
Cdd:TIGR02169 947 PEEELSLED-VQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
338-615 |
2.04e-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: 51.21 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 338 RRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----KQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQ 413
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 414 KE----FFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGEtsdtlnnvgyqgpTKMTKEELNALKStgdgTLDIR 489
Cdd:TIGR02168 318 LEeleaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE-------------LEAELEELESRLE----ELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 490 LKKLVDERECLLEQIKKLKGQ---LEERQKIGKLDNLRSEDDVLENGTDMHVMDLQrDANRQISDLKFKLAKSEQEITAL 566
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELEEELEELQEELERL 459
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 212276078 567 EQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 615
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
363-589 |
6.51e-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: 48.99 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 363 AEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVMLKEELKKHG 442
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA---ELRAELEAQKEELAELLRALYRLG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 443 IILNSEIATNGETSDTLNNVG--YQGPTKMTKEELNALKSTGDgtldiRLKKLVDERECLLEQIKKLKGQLEERQKigKL 520
Cdd:COG4942 118 RQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLA-----ELAALRAELEAERAELEALLAELEEERA--AL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 212276078 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 ... |
265-639 |
1.09e-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: 48.48 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 265 KELNELKDQIQDVEGKYMQGL-KEMKDSLAEVEEKYKkamvsnaQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEE 343
Cdd:TIGR04523 288 KQLNQLKSEISDLNNQKEQDWnKELKSELKNQEKKLE-------EIQNQISQNNKIISQLNEQISQLKKELTNSESENSE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 344 KNKEFErEKHAhsilqfqfaEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSE 423
Cdd:TIGR04523 361 KQRELE-EKQN---------EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE---LLEKE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 424 RDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQGPTKM--TKEELNALKSTGDgtldiRLKKLVDERECLL 501
Cdd:TIGR04523 428 IERLKETIIKNNSEIKD----LTNQDSVKELIIKNLDNTRESLETQLkvLSRSINKIKQNLE-----QKQKELKSKEKEL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 502 EQIKKLKGQLEERQK---------IGKLDNLRSEDDVLENGTDmhvmDLQRDANRQISDLKFKLAksEQEITALEQNVIR 572
Cdd:TIGR04523 499 KKLNEEKKELEEKVKdltkkisslKEKIEKLESEKKEKESKIS----DLEDELNKDDFELKKENL--EKEIDEKNKEIEE 572
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 212276078 573 LESQVSRYKSAAENAEKIEDELKAEKRKLQRELrsaldktEELEVSNGHLVKRLEKMKANRSALLSQ 639
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSI 632
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
363-616 |
1.63e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 363 AEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETiewKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKHG 442
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEK---RDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 443 IILNSEIATNGETSDTLNNVGYQGPTKMT-KEELNALKSTGDgTLDIRLKKlvdEREcLLEQIKKLKGQLEERQKI---- 517
Cdd:COG1340 85 EKLNELREELDELRKELAELNKAGGSIDKlRKEIERLEWRQQ-TEVLSPEE---EKE-LVEKIKELEKELEKAKKAlekn 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 518 GKLDNLRSEDDVLENGTDMHVMDLQRDANrQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAE 597
Cdd:COG1340 160 EKLKELRAELKELRKEAEEIHKKIKELAE-EAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
250
....*....|....*....
gi 212276078 598 KRKLQRELRSALDKTEELE 616
Cdd:COG1340 239 LRELRKELKKLRKKQRALK 257
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
280-640 |
1.90e-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: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 280 KYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQ 359
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 360 FQFAEVKEAL------KQREEMLEEIRQLQQKQassiREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVM 433
Cdd:TIGR04523 288 KQLNQLKSEIsdlnnqKEQDWNKELKSELKNQE----KKLEEIQNQISQNNKIISQLNEQIS---QLKKELTNSESENSE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 434 LKEELKKHGIILNSEIATNGETSDTLNNVGYQGPTKMTK----EELNALKstgdgtlDIRLKKLVDERECLLEQIKKLKG 509
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKiqnqEKLNQQK-------DEQIKKLQQEKELLEKEIERLKE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 510 QLEERQKigKLDNLRSEDDVLENGTDMH----------VMDLQRDANRQISDLKFK---LAKSEQEITALEQNVIRLESQ 576
Cdd:TIGR04523 434 TIIKNNS--EIKDLTNQDSVKELIIKNLdntresletqLKVLSRSINKIKQNLEQKqkeLKSKEKELKKLNEEKKELEEK 511
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212276078 577 VSRYKSAAENAEKIEDELKAEKRKLQRELRSALD---------KTEELEVSNGHLVKRLEKMKANRSALLSQQ 640
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKEKESKISDLEDelnkddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQ 584
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
256-596 |
1.93e-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: 48.14 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 256 DTEASIREI-KELNELKDQIQDVEgkymqglKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVdtlKDMLLELEEQL 334
Cdd:TIGR02169 234 ALERQKEAIeRQLASLEEELEKLT-------EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV---KEKIGELEAEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 335 AESRRQYEEKNKEFERekhAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQk 414
Cdd:TIGR02169 304 ASLERSIAEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 415 efFDSVRSERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQgptkmTKEELNALKStgdgtldiRLKKLV 494
Cdd:TIGR02169 380 --FAETRDELKDYREKLEKLKREINE----LKRELDRLQEELQRLSEELAD-----LNAAIAGIEA--------KINELE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 495 DERECLLEQIKKLKGQLEERQKIGKldnlrseddvlengtdmhvmdlqrDANRQISDLKFKLAKSEQEITALEQNVIRLE 574
Cdd:TIGR02169 441 EEKEDKALEIKKQEWKLEQLAADLS------------------------KYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
330 340
....*....|....*....|..
gi 212276078 575 SQVSRYKSAAENAEKIEDELKA 596
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEVLKA 518
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
361-640 |
2.58e-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: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 361 QFAEVKEALKQRE--EMLEEIRQLQQKQASSIREISDLQETIE----WKDKKIGALERQKEFFDSVRSERDDLREEVVML 434
Cdd:COG1196 214 RYRELKEELKELEaeLLLLKLRELEAELEELEAELEELEAELEeleaELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 435 KEELKKHGIILNSEIATNGETSDTLNNvgyqgptkmTKEELNALKSTGDG------TLDIRLKKLVDERECLLEQIKKLK 508
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEE---------LEEELAELEEELEEleeeleELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 509 GQLEERQKIgKLDNLRSEDDVLENgtDMHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAE 588
Cdd:COG1196 365 EALLEAEAE-LAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 212276078 589 KIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 640
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
367-603 |
2.63e-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: 47.37 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 367 EALKQREEMLE---EIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFD----SVRSERDDLREEVVMLKEELK 439
Cdd:TIGR02169 288 EQLRVKEKIGEleaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEreieEERKRRDKLTEEYAELKEELE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 440 KHGIILNSEIATNGETSDTLnnVGYQGPTKMTKEELNALKSTGDGTLDiRLKKLVDERECLLEQIKKLKGQLEERqkigk 519
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDEL--KDYREKLEKLKREINELKRELDRLQE-ELQRLSEELADLNAAIAGIEAKINEL----- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 520 ldnlrseDDVLEngtdmhvmdlqrdanrqisDLKFKLAKSEQEITALEQNVIRLESQVSRYKsaaENAEKIEDELKAEKR 599
Cdd:TIGR02169 440 -------EEEKE-------------------DKALEIKKQEWKLEQLAADLSKYEQELYDLK---EEYDRVEKELSKLQR 490
|
....
gi 212276078 600 KLQR 603
Cdd:TIGR02169 491 ELAE 494
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
265-633 |
2.80e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 265 KELNELKDQIQDVE-GKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKdmlLELEEQLAESRRQYEE 343
Cdd:PRK03918 372 EELERLKKRLTGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK---KAKGKCPVCGRELTEE 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 344 KNKEFEREKHAH-SILQFQFAEVKEALKQREEMLEEIRQL--QQKQASSIREISDLQETIEWKDKKIGA--LERQKEFFD 418
Cdd:PRK03918 449 HRKELLEEYTAElKRIEKELKEIEEKERKLRKELRELEKVlkKESELIKLKELAEQLKELEEKLKKYNLeeLEKKAEEYE 528
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 419 SVRSERDDLREEVVMLKEELKKHGIILNSEIATN----------GETSDTLNNVGYqGPTKMTKEELNALKSTGDGTldI 488
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEkkldeleeelAELLKELEELGF-ESVEELEERLKELEPFYNEY--L 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 489 RLKKLVDERECLLEQIKKLKGQLEErqkigKLDNLRSEDDVLEngtdmhvmdlqrDANRQISDLKFKLakSEQEITALEQ 568
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELDK-----AFEELAETEKRLE------------ELRKELEELEKKY--SEEEYEELRE 666
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212276078 569 NVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVsnghLVKRLEKMKANR 633
Cdd:PRK03918 667 EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
261-636 |
3.02e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 261 IREIKELNELKDQIQDVEGKymqgLKEMKDSLAEVEEK---YKKAMVSNAQLDNEKTNFM-YQVDTLKDMLLELEEQlae 336
Cdd:PRK03918 327 EERIKELEEKEERLEELKKK----LKELEKRLEELEERhelYEEAKAKKEELERLKKRLTgLTPEKLEKELEELEKA--- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 337 sRRQYEEKNKEFEREKhahsilqfqfAEVKEALKQREEMLEEIRQLQQK----------------QASSIREISDLQETI 400
Cdd:PRK03918 400 -KEEIEEEISKITARI----------GELKKEIKELKKAIEELKKAKGKcpvcgrelteehrkelLEEYTAELKRIEKEL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 401 EWKDKKIGALERQKEFFDSVRSERDDLR------EEVVMLKEELKKHGIilnSEIATNGETSDTLNN--VGYQGPTKMTK 472
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESELIklkelaEQLKELEEKLKKYNL---EELEKKAEEYEKLKEklIKLKGEIKSLK 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 473 EELNALKStgdgtLDIRLKKLVDERECLLEQIKKLKGQLEERqKIGKLDNLRSEDDVLENGTDMHVMdlQRDANRQISDL 552
Cdd:PRK03918 546 KELEKLEE-----LKKKLAELEKKLDELEEELAELLKELEEL-GFESVEELEERLKELEPFYNEYLE--LKDAEKELERE 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 553 KFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDE-----LKAEKRKLQRELRSALDKTEELEVSNGHLVKRLE 627
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
....*....
gi 212276078 628 KMKANRSAL 636
Cdd:PRK03918 698 KLKEELEER 706
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
340-631 |
5.49e-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: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 340 QYEEKNKEFEREKHAHSILQFQFAEvkealKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALER-----QK 414
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEELR-----EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEeieelQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 415 EFFdSVRSERDDLREEVVMLKEELK---KHGIILNSEIATNGETSDTLnnvgyqgptkmtKEELNALKstgdgtldirlk 491
Cdd:TIGR02168 289 ELY-ALANEISRLEQQKQILRERLAnleRQLEELEAQLEELESKLDEL------------AEELAELE------------ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 492 klvderecllEQIKKLKGQLEERQKigKLDNLRSEDDVLENGtdmhvmdlQRDANRQISDLKFKLAKSEQEITALEQNVI 571
Cdd:TIGR02168 344 ----------EKLEELKEELESLEA--ELEELEAELEELESR--------LEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 212276078 572 RLESQVSRYKSAAENA-EKIEDELK----AEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 631
Cdd:TIGR02168 404 RLEARLERLEDRRERLqQEIEELLKkleeAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
342-459 |
5.72e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.39 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 342 EEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 421
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
|
90 100 110
....*....|....*....|....*....|....*...
gi 212276078 422 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 459
Cdd:COG2433 458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
353-608 |
8.08e-05 |
|
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: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 353 HAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERqkeffdsvrsERDDLREEVV 432
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----------EIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 433 MLKEELKKhgiiLNSEIATNGETSDTLNNVgyqgptkmtkeeLNAlKSTGD--GTLDIrLKKLVDERECLLEQIKKLKGQ 510
Cdd:COG3883 83 ERREELGE----RARALYRSGGSVSYLDVL------------LGS-ESFSDflDRLSA-LSKIADADADLLEELKADKAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 511 LEERQKigKLDNLRSEddvlengtdmhVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKI 590
Cdd:COG3883 145 LEAKKA--ELEAKLAE-----------LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
250
....*....|....*...
gi 212276078 591 EDELKAEKRKLQRELRSA 608
Cdd:COG3883 212 AAAAAAAAAAAAAAAAAA 229
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
342-532 |
1.19e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 342 EEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVR 421
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 422 sERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQGptKMTKEELNALKSTGDGTLDIRLKKLVDERECLL 501
Cdd:COG4717 133 -ELEALEAELAELPERLEE----LEERLEELRELEEELEELEAEL--AELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|.
gi 212276078 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 |
1.69e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 383 QQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVMLKEELKKhgiilnseiatngetsdtlnnv 462
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEK---ALLKQLAALERRIAALARRIRA---------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 463 gyqgptkmTKEELNALKStgdgtldiRLKKLVDERECLLEQIKKLKGQLEER----QKIGKLDNLrsedDVLENGTDMhv 538
Cdd:COG4942 74 --------LEQELAALEA--------ELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPL----ALLLSPEDF-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 539 mdlqRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVS 618
Cdd:COG4942 132 ----LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
250
....*....|....*...
gi 212276078 619 NGHLVKRLEKMKANRSAL 636
Cdd:COG4942 208 LAELAAELAELQQEAEEL 225
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
364-631 |
2.82e-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: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 364 EVKEALKQREeMLEEIRQLQQKQASSIREISDLQETIEWkdkkiGALERQKEFFDSVRSERDDLREEVVMLKEELKkhgi 443
Cdd:COG4913 243 ALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAA-----LRLWFAQRRLELLEAELEELRAELARLEAELE---- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 444 ilnseiatngetsdtlnnvgyqgptkmtkeelnalkstgdgTLDIRLKKLVDERECLLEQIKKLKGQleerqkigKLDNL 523
Cdd:COG4913 313 -----------------------------------------RLEARLDALREELDELEAQIRGNGGD--------RLEQL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 524 RSEDDVLENGTDmHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAekiEDELKAEKRKLQR 603
Cdd:COG4913 344 EREIERLERELE-ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA---LAEAEAALRDLRR 419
|
250 260
....*....|....*....|....*...
gi 212276078 604 ELRSALDKTEELEVSNGHLVKRLEKMKA 631
Cdd:COG4913 420 ELRELEAEIASLERRKSNIPARLLALRD 447
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
338-639 |
9.04e-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: 42.41 E-value: 9.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 338 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKI--GALERQKE 415
Cdd:pfam15921 568 RQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnAGSERLRA 647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 416 FFDsVRSERDDLREEVvmlkeelkkhgiilnseiatngetsdtlnnvgyqgptKMTKEELNALKSTgdgtLDIRLKKLVD 495
Cdd:pfam15921 648 VKD-IKQERDQLLNEV-------------------------------------KTSRNELNSLSED----YEVLKRNFRN 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 496 ERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLEnGTDMHVMDLQRDANRQIsdlkfklakseqeiTALEQNVIRLES 575
Cdd:pfam15921 686 KSEEMETTTNKLKMQLKSAQS--ELEQTRNTLKSME-GSDGHAMKVAMGMQKQI--------------TAKRGQIDALQS 748
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 212276078 576 QVSRYKSAAENAEKIEDELKAEKRKLQRELRS-ALDKTE---ELEVSNGHlVKRLEKMKANRSALLSQ 639
Cdd:pfam15921 749 KIQFLEEAMTNANKEKHFLKEEKNKLSQELSTvATEKNKmagELEVLRSQ-ERRLKEKVANMEVALDK 815
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
486-636 |
1.05e-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: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 486 LDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGTDMHVMDLQR-------------DANRQISDL 552
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSR--QISALRKDLARLEAEVEQLEERIAQlskelteleaeieELEERLEEA 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 553 KFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKAN 632
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
....
gi 212276078 633 RSAL 636
Cdd:TIGR02168 854 IESL 857
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
485-614 |
1.39e-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: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 485 TLDIRLKKLVDERECLLEQIKKLKGQLEERQK-----IGKLDNLRSEDDVLENGTDMHVMDLQRD--------ANRQISD 551
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEArleaaKTELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrNNKEYEA 93
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 212276078 552 LKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 614
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
308-630 |
1.49e-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: 42.03 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 308 QLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREkhahsiLQFQFAEVKEALKQREEMLEEI----RQLQ 383
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQ------LVLANSELTEARTERDQFSQESgnldDQLQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 384 QKQASSIREISDLQETIEwKDKKIGALERQKEF-FDSVRSERDDLREEVVMLKEELKKhgiiLNSEiaTNGETSDTLNNV 462
Cdd:pfam15921 381 KLLADLHKREKELSLEKE-QNKRLWDRDTGNSItIDHLRRELDDRNMEVQRLEALLKA----MKSE--CQGQMERQMAAI 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 463 gyQGPTKmTKEELNALKSTGDGTLDIrLKKLVDE---RECLLEQ----IKKLKGQLEERQKIGKLDNlrSEDDVLENGTD 535
Cdd:pfam15921 454 --QGKNE-SLEKVSSLTAQLESTKEM-LRKVVEEltaKKMTLESsertVSDLTASLQEKERAIEATN--AEITKLRSRVD 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 536 MHVMDLQ---------RDANRQISDLKFKLAKSEQEITALEQ---NVIRLESQVSRyKSAAENAEKIEDELKAEKRKLQ- 602
Cdd:pfam15921 528 LKLQELQhlknegdhlRNVQTECEALKLQMAEKDKVIEILRQqieNMTQLVGQHGR-TAGAMQVEKAQLEKEINDRRLEl 606
|
330 340 350
....*....|....*....|....*....|..
gi 212276078 603 RELRSALDKTE----ELEVSNGHLvkRLEKMK 630
Cdd:pfam15921 607 QEFKILKDKKDakirELEARVSDL--ELEKVK 636
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
321-634 |
1.86e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 321 DTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQEti 400
Cdd:pfam02463 208 KALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE-- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 401 EWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGEtsdtlnnvgyqgpTKMTKEELNALKS 480
Cdd:pfam02463 286 EELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEE-------------LEKELKELEIKRE 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 481 TGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKLDNlrseddvlENGTDMHVMDLQRDANRQISDLKFKLAKSE 560
Cdd:pfam02463 353 AEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE--------EELELKSEEEKEAQLLLELARQLEDLLKEE 424
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212276078 561 QEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRS 634
Cdd:pfam02463 425 KKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
368-566 |
1.90e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 368 ALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFF------DSVRSERDDLREEVVMLKEElkkh 441
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDAS---- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 442 giilNSEIATNGETSDTLnnvgyqgptkmtKEELNALKSTGDGtLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKL- 520
Cdd:COG4913 684 ----SDDLAALEEQLEEL------------EAELEELEEELDE-LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLe 746
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 212276078 521 DNLRSEDDVLENGTDMHVMDLQRDANRQISDLKFKLAKSEQEITAL 566
Cdd:COG4913 747 LRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
338-637 |
2.15e-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: 41.19 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 338 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFF 417
Cdd:TIGR00606 195 RQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKAL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 418 DSVRSERDDLREEVVMLKEELKKhgiilnseiATNGETSDTLNNvgyQGPTKMTKEELNALKSTGDGTLDIRLKKLVDER 497
Cdd:TIGR00606 275 KSRKKQMEKDNSELELKMEKVFQ---------GTDEQLNDLYHN---HQRTVREKERELVDCQRELEKLNKERRLLNQEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 498 ECLLEQIKKLKGQLEERQ-KIGKLDNLRseddvLENGTDMHVMDLQRDA--NRQISD-LKFKLAKSEQEITALEQNVIRL 573
Cdd:TIGR00606 343 TELLVEQGRLQLQADRHQeHIRARDSLI-----QSLATRLELDGFERGPfsERQIKNfHTLVIERQEDEAKTAAQLCADL 417
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 212276078 574 ESQVsryKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEvsngHLVKRLEKMKANRSALL 637
Cdd:TIGR00606 418 QSKE---RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELK----FVIKELQQLEGSSDRIL 474
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
489-640 |
2.52e-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: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 489 RLKKLVDERECLLEQIKKLKGQLEE-----RQKIGKLDNLRSEDDVLEN------GTDMHVMDLQRDANRQISDLKFKLA 557
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEEltaelQELEEKLEELRLEVSELEEeieelqKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 558 KSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALL 637
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
...
gi 212276078 638 SQQ 640
Cdd:TIGR02168 393 LQI 395
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
361-440 |
3.14e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 40.44 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 361 QFAEVKEALKQR--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 438
Cdd:PRK05431 10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89
|
..
gi 212276078 439 KK 440
Cdd:PRK05431 90 DE 91
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
358-630 |
3.56e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 358 LQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEE 437
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 438 LKKHGIILnseiatnGETSDTLNNVgyqgptkmtKEELNALKST--------GDGTLDIRLKKLVDERECLLEQIKKLKG 509
Cdd:PRK03918 254 KRKLEEKI-------RELEERIEEL---------KKEIEELEEKvkelkelkEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 510 QLEER-----QKIGKLDNLRSEDDVLENgtdmhvmdLQRDANRQISDLKfKLAKSEQEITALEQNVIRLESQVSRYKsaA 584
Cdd:PRK03918 318 RLEEEingieERIKELEEKEERLEELKK--------KLKELEKRLEELE-ERHELYEEAKAKKEELERLKKRLTGLT--P 386
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 212276078 585 ENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMK 630
Cdd:PRK03918 387 EKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
236-429 |
6.33e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.65 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 236 LASLGGTSSRRGSGDTSISIDTEASIREIKELNELKDQIQDVEGKYMQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTN 315
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 316 FMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEM-LEEIRQLQQKQASSIREIS 394
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLtLEEAEALENKIEDDEEEAR 971
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 212276078 395 DLQETIEWKDKKIGA--------LERQKEFFDSVRSERDDLRE 429
Cdd:TIGR02168 972 RRLKRLENKIKELGPvnlaaieeYEELKERYDFLTAQKEDLTE 1014
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
262-614 |
6.42e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.66 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 262 REIKELNELKDQIQDVEGKymqgLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES--RR 339
Cdd:PRK03918 228 KEVKELEELKEEIEELEKE----LESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSefYE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 340 QYEEKNKEFEREKhahSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEW---------------KD 404
Cdd:PRK03918 304 EYLDELREIEKRL---SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyeeakakkeelerlkKR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 405 KKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQGP------TKMTKEELNAL 478
Cdd:PRK03918 381 LTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE----LKKEIKELKKAIEELKKAKGKCPvcgrelTEEHRKELLEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 479 KSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKLDNLRSEDDVLENGTDMHVMDLQRDANRQISDLKFKLAK 558
Cdd:PRK03918 457 YTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK 536
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 212276078 559 SEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 614
Cdd:PRK03918 537 LKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEE 592
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
258-440 |
6.66e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 39.65 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 258 EASIREIKELNELKDQIQdvegkymQGLKEMKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES 337
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 338 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREemlEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFF 417
Cdd:TIGR02168 343 EEKLEELKEELESLEAELEELEAELEELESRLEELE---EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
170 180 190
....*....|....*....|....*....|..
gi 212276078 418 DS---------VRSERDDLREEVVMLKEELKK 440
Cdd:TIGR02168 420 QQeieellkklEEAELKELQAELEELEEELEE 451
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
581-640 |
7.73e-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: 7.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 581 KSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 640
Cdd:pfam11932 27 AAAAQSQKKI-DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQI 85
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
469-640 |
7.78e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 39.65 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 469 KMTKEELNALKSTGDGTLDIRLKKLVDEREcllEQIKKLKGQLEE--RQKIGKLDNLRSEDDVLEngtdmHVMDLQRDAN 546
Cdd:PRK10929 79 KLSAELRQQLNNERDEPRSVPPNMSTDALE---QEILQVSSQLLEksRQAQQEQDRAREISDSLS-----QLPQQQTEAR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 547 RQISDLKFKL--------AKSEQEITALEQNVIRLESQVSRYKSA--------------AENAEKIEDELKAEKRKL--- 601
Cdd:PRK10929 151 RQLNEIERRLqtlgtpntPLAQAQLTALQAESAALKALVDELELAqlsannrqelarlrSELAKKRSQQLDAYLQALrnq 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 212276078 602 -----QRELRSALDKTEELEVSNGHLVKRL-EKMKANR--SALLSQQ 640
Cdd:PRK10929 231 lnsqrQREAERALESTELLAEQSGDLPKSIvAQFKINRelSQALNQQ 277
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
264-640 |
8.89e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 39.26 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 264 IKELNELKDQIQDVE---GKYMQGLKEMkDSLAEVEEKYKKAMVSNAQLDNEKTNF----------MYQVDTLKDMLLEL 330
Cdd:TIGR01612 1249 IEDLDEIKEKSPEIEnemGIEMDIKAEM-ETFNISHDDDKDHHIISKKHDENISDIrekslkiiedFSEESDINDIKKEL 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 331 EEQLAESRRQYEEKNKEFEREKHAHSILQFQ-----FAEVKEALKQREEMLEEIRQLQQKQASSIREISD---------- 395
Cdd:TIGR01612 1328 QKNLLDAQKHNSDINLYLNEIANIYNILKLNkikkiIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDdinleecksk 1407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 396 LQETIEWKDKKiGALERQKEFFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVGYQGPTKMtKEEL 475
Cdd:TIGR01612 1408 IESTLDDKDID-ECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNATNDH-DFNI 1485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 476 NALKSTGDGTldirlKKLVDERECLLEQIKKLKGQLEE-RQKIGKLDNLRSEDDVLENgtdmhVMDLQRDANRQISDLK- 553
Cdd:TIGR01612 1486 NELKEHIDKS-----KGCKDEADKNAKAIEKNKELFEQyKKDVTELLNKYSALAIKNK-----FAKTKKDSEIIIKEIKd 1555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 212276078 554 ------FKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKL------QRELRSALDKTEELE--VSN 619
Cdd:TIGR01612 1556 ahkkfiLEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFlkisdiKKKINDCLKETESIEkkISS 1635
|
410 420
....*....|....*....|.
gi 212276078 620 GHLVKRLEKMKANRSALLSQQ 640
Cdd:TIGR01612 1636 FSIDSQDTELKENGDNLNSLQ 1656
|
|
| |
