|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
212-541 |
1.65e-92 |
|
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: 287.36 E-value: 1.65e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 212 VEERPEKDFTE---------KGSRNMPGLSAATLASLGGTSSRRGSGDTSISIDTEASIREIKDSLAEVEEKYKKAMVSN 282
Cdd:pfam09738 30 VEENADRVFDMssssgadtaSGSPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKHELKEVEEKYRKAMISN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 283 AQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEeirqlqqkq 362
Cdd:pfam09738 110 AQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQLAELKEQLKQRDELIE--------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 363 assireisdlqetiewkdkkigalerqkeffdsvrserddlreevvmlkeelkKHGIILNSEIATNGEtsdTLNNVGYQG 442
Cdd:pfam09738 181 -----------------------------------------------------KHGLVIVPDENTNGE---EENSPADAK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 443 PTKMTKEELNALKSTGDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQ--KIGKLDNLRSEDDVLENGTdmHVMDLQRD 520
Cdd:pfam09738 205 RALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKskRNSTRSSQSPDGFGLENGS--HVIEVQRE 282
|
330 340
....*....|....*....|.
gi 2462578507 521 ANRQISDLKFKLAKSEQEITA 541
Cdd:pfam09738 283 ANKQISDYKFKLQKAEQEITT 303
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
235-591 |
1.28e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 235 TLASLGGTSSRRGSGDTSISIDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESR 314
Cdd:TIGR02168 653 DLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALR 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 315 RQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEirqLQQKQASSIREISDLQETIewkdkkigalERQKEFFD 394
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE---AEEELAEAEAEIEELEAQI----------EQLKEELK 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 395 SVRSERDDLREEVVMLKEELKKHGIILNSEIATNGETSDTLNNVGYQgpTKMTKEELNALKSTGDgTLDIRLKKLVDERE 474
Cdd:TIGR02168 800 ALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ--IEELSEDIESLAAEIE-ELEELIEELESELE 876
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 475 CLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGtdmhvmdlQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVS 554
Cdd:TIGR02168 877 ALLNERASLEEALALLRS--ELEELSEELRELESK--------RSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
330 340 350
....*....|....*....|....*....|....*...
gi 2462578507 555 -RYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 591
Cdd:TIGR02168 947 eEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
337-615 |
2.89e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.00 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 337 QFAEVKEALK-QREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGAL----ERQKEFFDSVRSERDDLREEVVMLK 411
Cdd:TIGR02169 678 RLRERLEGLKrELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeeEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 412 EELKKhgiiLNSEIAtngETSDTLNNVgyqgptkmtKEELNALKstgDGTLDIRLKKLVDERECLLEQIKKLKGQLEERQ 491
Cdd:TIGR02169 758 SELKE----LEARIE---ELEEDLHKL---------EEALNDLE---ARLSHSRIPEIQAELSKLEEEVSRIEARLREIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 492 KigKLDNLRSEDDVLEngtdmhvmDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELK 571
Cdd:TIGR02169 819 Q--KLNRLTLEKEYLE--------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLK 888
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2462578507 572 AEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQ 615
Cdd:TIGR02169 889 KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE 932
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
339-615 |
3.61e-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: 56.60 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 339 AEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQkefFDSVRSERDDLREEVVMLKEELKKhg 418
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER---IAQLSKELTELEAEIEELEERLEE-- 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 419 iiLNSEIATNGETSDTLnnvgyQGPTKMTKEELNALKSTGD------GTLDIRLKKLVDERECLLEQIKKLKGQLEERQK 492
Cdd:TIGR02168 773 --AEEELAEAEAEIEEL-----EAQIEQLKEELKALREALDelraelTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 493 IGKldnlRSEDDVLEngtdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKA 572
Cdd:TIGR02168 846 QIE----ELSEDIES-------------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2462578507 573 EKRKLQRELrsaldktEELEVSNGHLVKRLEKMKANRSALLSQ 615
Cdd:TIGR02168 909 KRSELRREL-------EELREKLAQLELRLEGLEVRIDNLQER 944
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
262-592 |
2.64e-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: 53.92 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 262 REIKDSLAEVEEKYKKamvsnaqLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQFQFAEV 341
Cdd:TIGR02169 670 RSEPAELQRLRERLEG-------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 342 KEALKQREEMLEEIRQLQQKQASsirEISDLQETIEWKDKKIGALERQ--KEFFDSVRSERDDLREEVVMLKEELKKHGI 419
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEA---RIEELEEDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 420 ILNSEIATNGETSDTLNNVgyQGPTKMTKEELNALKSTGDgTLDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNL 499
Cdd:TIGR02169 820 KLNRLTLEKEYLEKEIQEL--QEQRIDLKEQIKSIEKEIE-NLNGKKEELEEELEELEAALRDLESRLGDLKK--ERDEL 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 500 RSEDDVLENGTDMHVMDLQRdANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSA---AENAEKIE--------- 567
Cdd:TIGR02169 895 EAQLRELERKIEELEAQIEK-KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLedvQAELQRVEeeiralepv 973
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2462578507 568 ---------------DELKAEKRKLQRELRSALDKTEELE 592
Cdd:TIGR02169 974 nmlaiqeyeevlkrlDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
339-613 |
6.60e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.76 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 339 AEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWK-------DKKIGALER-----QKEFFDSVRSERDDLREE 406
Cdd:TIGR02169 716 RKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVkselkelEARIEELEEdlhklEEALNDLEARLSHSRIPE 795
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 407 VVMLKEELKK-HGIILNSEIATNGETSDTLNNVGYQGPTKMTKEELNALkstgdgtLDIRLKKLVDERECLLEQIKKLKG 485
Cdd:TIGR02169 796 IQAELSKLEEeVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID-------LKEQIKSIEKEIENLNGKKEELEE 868
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 486 QLEE-----RQKIGKLDNLRSEDDVLENgtDMHVM-DLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSA 559
Cdd:TIGR02169 869 ELEEleaalRDLESRLGDLKKERDELEA--QLRELeRKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462578507 560 AENAEKIEDeLKAEKRKLQRELRS-------ALDKTEELEVSNGHLVKRLEKMKANRSALL 613
Cdd:TIGR02169 947 PEEELSLED-VQAELQRVEEEIRAlepvnmlAIQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
314-591 |
1.62e-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: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 314 RRQYEEKNKEFEREKHAHSILQFQFAEVKEAL----KQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQ 389
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLeelrLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 390 KE----FFDSVRSERDDLREEVVMLKEELKKHGIILNSEIATNGEtsdtlnnvgyqgpTKMTKEELNALKStgdgTLDIR 465
Cdd:TIGR02168 318 LEeleaQLEELESKLDELAEELAELEEKLEELKEELESLEAELEE-------------LEAELEELESRLE----ELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 466 LKKLVDERECLLEQIKKLKGQ---LEERQKIGKLDNLRSEDDVLENGTDMHVMDLQrDANRQISDLKFKLAKSEQEITAL 542
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEierLEARLERLEDRRERLQQEIEELLKKLEEAELK-ELQAELEELEEELEELQEELERL 459
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2462578507 543 EQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEEL 591
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV 508
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
339-565 |
4.88e-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: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 339 AEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVMLKEELKKHG 418
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA---ELRAELEAQKEELAELLRALYRLG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 419 IILNSEIATNGETSDTLNNVG--YQGPTKMTKEELNALKSTGDgtldiRLKKLVDERECLLEQIKKLKGQLEERQKigKL 496
Cdd:COG4942 118 RQPPLALLLSPEDFLDAVRRLqyLKYLAPARREQAEELRADLA-----ELAALRAELEAERAELEALLAELEEERA--AL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578507 497 DNLRSEddvlengtdmhvmdlqrdANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEK 565
Cdd:COG4942 191 EALKAE------------------RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
339-592 |
6.69e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 339 AEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETiewKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKHG 418
Cdd:COG1340 8 SSLEELEEKIEELREEIEELKEKRDELNEELKELAEK---RDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 419 IILNSEIATNGETSDTLNNVGYQGPTKMT-KEELNALKSTGDgTLDIRLKKlvdEREcLLEQIKKLKGQLEERQKI---- 493
Cdd:COG1340 85 EKLNELREELDELRKELAELNKAGGSIDKlRKEIERLEWRQQ-TEVLSPEE---EKE-LVEKIKELEKELEKAKKAlekn 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 494 GKLDNLRSEDDVLENGTDMHVMDLQRDANrQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAE 573
Cdd:COG1340 160 EKLKELRAELKELRKEAEEIHKKIKELAE-EAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKE 238
|
250
....*....|....*....
gi 2462578507 574 KRKLQRELRSALDKTEELE 592
Cdd:COG1340 239 LRELRKELKKLRKKQRALK 257
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
343-579 |
1.80e-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: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 343 EALKQREEMLE---EIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFD----SVRSERDDLREEVVMLKEELK 415
Cdd:TIGR02169 288 EQLRVKEKIGEleaEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEreieEERKRRDKLTEEYAELKEELE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 416 KHGIILNSEIATNGETSDTLnnVGYQGPTKMTKEELNALKSTGDGTLDiRLKKLVDERECLLEQIKKLKGQLEERqkigk 495
Cdd:TIGR02169 368 DLRAELEEVDKEFAETRDEL--KDYREKLEKLKREINELKRELDRLQE-ELQRLSEELADLNAAIAGIEAKINEL----- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 496 ldnlrseDDVLEngtdmhvmdlqrdanrqisDLKFKLAKSEQEITALEQNVIRLESQVSRYKsaaENAEKIEDELKAEKR 575
Cdd:TIGR02169 440 -------EEEKE-------------------DKALEIKKQEWKLEQLAADLSKYEQELYDLK---EEYDRVEKELSKLQR 490
|
....
gi 2462578507 576 KLQR 579
Cdd:TIGR02169 491 ELAE 494
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
258-609 |
1.82e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 258 EASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKdmlLELEEQLAESRRQYEEKNKEFEREKHAH-SILQF 336
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK---KAKGKCPVCGRELTEEHRKELLEEYTAElKRIEK 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 337 QFAEVKEALKQREEMLEEIRQL--QQKQASSIREISDLQETIEWKDKKIGA--LERQKEFFDSVRSERDDLREEVVMLKE 412
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVlkKESELIKLKELAEQLKELEEKLKKYNLeeLEKKAEEYEKLKEKLIKLKGEIKSLKK 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 413 ELKKHGIILNSEIATN----------GETSDTLNNVGYqGPTKMTKEELNALKSTGDGTldIRLKKLVDERECLLEQIKK 482
Cdd:PRK03918 547 ELEKLEELKKKLAELEkkldeleeelAELLKELEELGF-ESVEELEERLKELEPFYNEY--LELKDAEKELEREEKELKK 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 483 LKGQLEErqkigKLDNLRSEDDVLEngtdmhvmdlqrDANRQISDLKFKLakSEQEITALEQNVIRLESQVSRYKSAAEN 562
Cdd:PRK03918 624 LEEELDK-----AFEELAETEKRLE------------ELRKELEELEKKY--SEEEYEELREEYLELSRELAGLRAELEE 684
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2462578507 563 AEKIEDELKAEKRKLQRELRSALDKTEELEVsnghLVKRLEKMKANR 609
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
340-616 |
2.14e-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: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 340 EVKEALKQREEmleEIRQLQQKQASSIREISDLQETIEwkdkkigalerqkeffdSVRSERDDLREEVVMLKEELKKHGI 419
Cdd:TIGR04523 311 ELKSELKNQEK---KLEEIQNQISQNNKIISQLNEQIS-----------------QLKKELTNSESENSEKQRELEEKQN 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 420 ILNSEIATNGETSDTLNNVGYQGPTKMTK----EELNALKstgdgtlDIRLKKLVDERECLLEQIKKLKGQLEERQKigK 495
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIKNLESQINDLESKiqnqEKLNQQK-------DEQIKKLQQEKELLEKEIERLKETIIKNNS--E 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 496 LDNLRSEDDVLENGTDMH----------VMDLQRDANRQISDLKFK---LAKSEQEITALEQNVIRLESQVSRYKSAAEN 562
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLdntresletqLKVLSRSINKIKQNLEQKqkeLKSKEKELKKLNEEKKELEEKVKDLTKKISS 521
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462578507 563 AEKIEDELKAEKRKLQRELRSALD---------KTEELEVSNGHLVKRLEKMKANRSALLSQQ 616
Cdd:TIGR04523 522 LKEKIEKLESEKKEKESKISDLEDelnkddfelKKENLEKEIDEKNKEIEELKQTQKSLKKKQ 584
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
337-616 |
2.32e-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: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 337 QFAEVKEALKQRE--EMLEEIRQLQQKQASSIREISDLQETIE----WKDKKIGALERQKEFFDSVRSERDDLREEVVML 410
Cdd:COG1196 214 RYRELKEELKELEaeLLLLKLRELEAELEELEAELEELEAELEeleaELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 411 KEELKKHGIILNSEIATNGETSDTLNNvgyqgptkmTKEELNALKSTGDG------TLDIRLKKLVDERECLLEQIKKLK 484
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERLEE---------LEEELAELEEELEEleeeleELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 485 GQLEERQKIgKLDNLRSEDDVLENgtDMHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAE 564
Cdd:COG1196 365 EALLEAEAE-LAEAEEELEELAEE--LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2462578507 565 KIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 616
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL 493
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
316-607 |
3.76e-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: 46.97 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 316 QYEEKNKEFEREKHAHSILQFQFAEvkealKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALER-----QK 390
Cdd:TIGR02168 214 RYKELKAELRELELALLVLRLEELR-----EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEeieelQK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 391 EFFdSVRSERDDLREEVVMLKEELK---KHGIILNSEIATNGETSDTLnnvgyqgptkmtKEELNALKstgdgtldirlk 467
Cdd:TIGR02168 289 ELY-ALANEISRLEQQKQILRERLAnleRQLEELEAQLEELESKLDEL------------AEELAELE------------ 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 468 klvderecllEQIKKLKGQLEERQKigKLDNLRSEDDVLENGtdmhvmdlQRDANRQISDLKFKLAKSEQEITALEQNVI 547
Cdd:TIGR02168 344 ----------EKLEELKEELESLEA--ELEELEAELEELESR--------LEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462578507 548 RLESQVSRYKSAAENA-EKIEDELK----AEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKA 607
Cdd:TIGR02168 404 RLEARLERLEDRRERLqQEIEELLKkleeAELKELQAELEELEEELEELQEELERLEEALEELRE 468
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
318-435 |
5.52e-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: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 318 EEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRqlqqkqassiREISDLQETIEWKDKKIGALERQKEFFDSVR 397
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELEEKDERIERLERELSEARSEE 457
|
90 100 110
....*....|....*....|....*....|....*...
gi 2462578507 398 SERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTL 435
Cdd:COG2433 458 RREIRKDREISRLDREIER----LERELEEERERIEEL 491
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
251-615 |
6.36e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 251 TSISIDTEASIREIKDSLAEVEEKYKKAMVSNAQ-----------------LDNEK---TNFMYQVDTLKDMLLELEEQL 310
Cdd:pfam15921 485 TAKKMTLESSERTVSDLTASLQEKERAIEATNAEitklrsrvdlklqelqhLKNEGdhlRNVQTECEALKLQMAEKDKVI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 311 AESRRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKI--GALER 388
Cdd:pfam15921 565 EILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnAGSER 644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 389 QKEFFDsVRSERDDLREEVvmlkeelkkhgiilnseiatngetsdtlnnvgyqgptKMTKEELNALKSTgdgtLDIRLKK 468
Cdd:pfam15921 645 LRAVKD-IKQERDQLLNEV-------------------------------------KTSRNELNSLSED----YEVLKRN 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 469 LVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLEnGTDMHVMDLQRDANRQIsdlkfklakseqeiTALEQNVIR 548
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLKSAQS--ELEQTRNTLKSME-GSDGHAMKVAMGMQKQI--------------TAKRGQIDA 745
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462578507 549 LESQVSRYKSAAENAEKIEDELKAEKRKLQRELRS-ALDKTE---ELEVSNGHlVKRLEKMKANRSALLSQ 615
Cdd:pfam15921 746 LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTvATEKNKmagELEVLRSQ-ERRLKEKVANMEVALDK 815
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
329-584 |
6.73e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 329 HAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERqkeffdsvrsERDDLREEVV 408
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA----------EIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 409 MLKEELKKhgiiLNSEIATNGETSDTLNNVgyqgptkmtkeeLNAlKSTGD--GTLDIrLKKLVDERECLLEQIKKLKGQ 486
Cdd:COG3883 83 ERREELGE----RARALYRSGGSVSYLDVL------------LGS-ESFSDflDRLSA-LSKIADADADLLEELKADKAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 487 LEERQKigKLDNLRSEddvlengtdmhVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKI 566
Cdd:COG3883 145 LEAKKA--ELEAKLAE-----------LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
250
....*....|....*...
gi 2462578507 567 EDELKAEKRKLQRELRSA 584
Cdd:COG3883 212 AAAAAAAAAAAAAAAAAA 229
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
318-508 |
9.32e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 9.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 318 EEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVR 397
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 398 sERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQGptKMTKEELNALKSTGDGTLDIRLKKLVDERECLL 477
Cdd:COG4717 133 -ELEALEAELAELPERLEE----LEERLEELRELEEELEELEAEL--AELQEELEELLEQLSLATEEELQDLAEELEELQ 205
|
170 180 190
....*....|....*....|....*....|.
gi 2462578507 478 EQIKKLKGQLEERQKigKLDNLRSEDDVLEN 508
Cdd:COG4717 206 QRLAELEEELEEAQE--ELEELEEELEQLEN 234
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
314-572 |
1.10e-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: 45.44 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 314 RRQYEEKNKEFERekhAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQkefF 393
Cdd:TIGR02169 307 ERSIAEKERELED---AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE---F 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 394 DSVRSERDDLREEVVMLKEELKKhgiiLNSEIATNGETSDTLNNVGYQgptkmTKEELNALKStgdgtldiRLKKLVDER 473
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINE----LKRELDRLQEELQRLSEELAD-----LNAAIAGIEA--------KINELEEEK 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 474 ECLLEQIKKLKGQLEERQKIGKldnlrseddvlengtdmhvmdlqrDANRQISDLKFKLAKSEQEITALEQNVIRLESQV 553
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLS------------------------KYEQELYDLKEEYDRVEKELSKLQRELAEAEAQA 499
|
250
....*....|....*....
gi 2462578507 554 SRYKSAAENAEKIEDELKA 572
Cdd:TIGR02169 500 RASEERVRGGRAVEEVLKA 518
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
359-612 |
1.30e-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: 44.75 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 359 QQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVMLKEELKKhgiilnseiatngetsdtlnnv 438
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEK---ALLKQLAALERRIAALARRIRA---------------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 439 gyqgptkmTKEELNALKStgdgtldiRLKKLVDERECLLEQIKKLKGQLEER----QKIGKLDNLrsedDVLENGTDMhv 514
Cdd:COG4942 74 --------LEQELAALEA--------ELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPL----ALLLSPEDF-- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 515 mdlqRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVS 594
Cdd:COG4942 132 ----LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE 207
|
250
....*....|....*...
gi 2462578507 595 NGHLVKRLEKMKANRSAL 612
Cdd:COG4942 208 LAELAAELAELQQEAEEL 225
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
340-607 |
2.70e-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: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 340 EVKEALKQREeMLEEIRQLQQKQASSIREISDLQETIEWkdkkiGALERQKEFFDSVRSERDDLREEVVMLKEELKkhgi 419
Cdd:COG4913 243 ALEDAREQIE-LLEPIRELAERYAAARERLAELEYLRAA-----LRLWFAQRRLELLEAELEELRAELARLEAELE---- 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 420 ilnseiatngetsdtlnnvgyqgptkmtkeelnalkstgdgTLDIRLKKLVDERECLLEQIKKLKGQleerqkigKLDNL 499
Cdd:COG4913 313 -----------------------------------------RLEARLDALREELDELEAQIRGNGGD--------RLEQL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 500 RSEDDVLENGTDmHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAekiEDELKAEKRKLQR 579
Cdd:COG4913 344 EREIERLERELE-ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA---LAEAEAALRDLRR 419
|
250 260
....*....|....*....|....*...
gi 2462578507 580 ELRSALDKTEELEVSNGHLVKRLEKMKA 607
Cdd:COG4913 420 ELRELEAEIASLERRKSNIPARLLALRD 447
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
462-612 |
7.64e-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: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 462 LDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGTDMHVMDLQR-------------DANRQISDL 528
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSR--QISALRKDLARLEAEVEQLEERIAQlskelteleaeieELEERLEEA 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 529 KFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKAN 608
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED 853
|
....
gi 2462578507 609 RSAL 612
Cdd:TIGR02168 854 IESL 857
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
255-610 |
7.73e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.65 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 255 IDTEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAES--------RRQYEEKNKEFER 326
Cdd:pfam02463 158 IEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKekleleeeYLLYLDYLKLNEE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 327 EKHAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQEtiEWKDKKIGALERQKEFFDSVRSERDDLREE 406
Cdd:pfam02463 238 RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE--EELKLLAKEEEELKSELLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 407 VVMLKEELKKHGIILNSEIATNGEtsdtlnnvgyqgpTKMTKEELNALKSTGDGTLDIRLKKLVDERECLLEQIKKLKGQ 486
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEE-------------LEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 487 LEERQKIGKLDNlrseddvlENGTDMHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKI 566
Cdd:pfam02463 383 SERLSSAAKLKE--------EELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELE 454
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2462578507 567 EDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRS 610
Cdd:pfam02463 455 KQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER 498
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
353-611 |
9.19e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 353 EEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQkeffdsvrseRDDLREEVVMLKEELKKhgiilnseiatngets 432
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ----------LAALERRIAALARRIRA---------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 433 dtlnnvgyqgptkmTKEELNALKStgdgtldiRLKKLVDERECLLEQIKKLKGQLEER----QKIGKLDNLR---SEDDV 505
Cdd:COG4942 74 --------------LEQELAALEA--------ELAELEKEIAELRAELEAQKEELAELlralYRLGRQPPLAlllSPEDF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 506 LENGTDMHVMD-LQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSA 584
Cdd:COG4942 132 LDAVRRLQYLKyLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL 211
|
250 260
....*....|....*....|....*..
gi 2462578507 585 LDKTEELEVSNGHLVKRLEKMKANRSA 611
Cdd:COG4942 212 AAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
261-615 |
1.04e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 261 IREIKDSLAEVEEKYKkamvsnaQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFErEKHAhsilqfqfaE 340
Cdd:TIGR04523 309 NKELKSELKNQEKKLE-------EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE-EKQN---------E 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 341 VKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEffdSVRSERDDLREEVVMLKEELKKhgii 420
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE---LLEKEIERLKETIIKNNSEIKD---- 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 421 LNSEIATNGETSDTLNNVGYQGPTKM--TKEELNALKSTGDgtldiRLKKLVDERECLLEQIKKLKGQLEERQK------ 492
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLkvLSRSINKIKQNLE-----QKQKELKSKEKELKKLNEEKKELEEKVKdltkki 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 493 ---IGKLDNLRSEDDVLENGTDmhvmDLQRDANRQISDLKFKLAksEQEITALEQNVIRLESQVSRYKSAAENAEKIEDE 569
Cdd:TIGR04523 520 sslKEKIEKLESEKKEKESKIS----DLEDELNKDDFELKKENL--EKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQ 593
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 2462578507 570 LKAEKRKLQRELrsaldktEELEVSNGHLVKRLEKMKANRSALLSQ 615
Cdd:TIGR04523 594 KEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSI 632
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
462-590 |
1.05e-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: 41.06 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 462 LDIRLKKLVDERECLLEQIKKLKGQLEERQKigKLDNLRSEDDVLENGTDMHVMDLQRD--------ANRQISDLKFKLA 533
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAAKT--ELEDLEKEIKRLELEIEEVEARIKKYeeqlgnvrNNKEYEALQKEIE 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2462578507 534 KSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEE 590
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
284-606 |
1.14e-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: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 284 QLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREkhahsiLQFQFAEVKEALKQREEMLEEI----RQLQ 359
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQ------LVLANSELTEARTERDQFSQESgnldDQLQ 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 360 QKQASSIREISDLQETIEwKDKKIGALERQKEF-FDSVRSERDDLREEVVMLKEELKKhgiiLNSEiaTNGETSDTLNNV 438
Cdd:pfam15921 381 KLLADLHKREKELSLEKE-QNKRLWDRDTGNSItIDHLRRELDDRNMEVQRLEALLKA----MKSE--CQGQMERQMAAI 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 439 gyQGPTKmTKEELNALKSTGDGTLDIrLKKLVDE---RECLLEQ----IKKLKGQLEERQKIGKLDNlrSEDDVLENGTD 511
Cdd:pfam15921 454 --QGKNE-SLEKVSSLTAQLESTKEM-LRKVVEEltaKKMTLESsertVSDLTASLQEKERAIEATN--AEITKLRSRVD 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 512 MHVMDLQ---------RDANRQISDLKFKLAKSEQEITALEQ---NVIRLESQVSRyKSAAENAEKIEDELKAEKRKLQ- 578
Cdd:pfam15921 528 LKLQELQhlknegdhlRNVQTECEALKLQMAEKDKVIEILRQqieNMTQLVGQHGR-TAGAMQVEKAQLEKEINDRRLEl 606
|
330 340 350
....*....|....*....|....*....|..
gi 2462578507 579 RELRSALDKTE----ELEVSNGHLvkRLEKMK 606
Cdd:pfam15921 607 QEFKILKDKKDakirELEARVSDL--ELEKVK 636
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
314-613 |
1.28e-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: 41.96 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 314 RRQYEEKNKEFEREKHAHSILQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFF 393
Cdd:TIGR00606 195 RQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKAL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 394 DSVRSERDDLREEVVMLKEELKKhgiilnseiATNGETSDTLNNvgyQGPTKMTKEELNALKSTGDGTLDIRLKKLVDER 473
Cdd:TIGR00606 275 KSRKKQMEKDNSELELKMEKVFQ---------GTDEQLNDLYHN---HQRTVREKERELVDCQRELEKLNKERRLLNQEK 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 474 ECLLEQIKKLKGQLEERQ-KIGKLDNLRseddvLENGTDMHVMDLQRDA--NRQISD-LKFKLAKSEQEITALEQNVIRL 549
Cdd:TIGR00606 343 TELLVEQGRLQLQADRHQeHIRARDSLI-----QSLATRLELDGFERGPfsERQIKNfHTLVIERQEDEAKTAAQLCADL 417
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462578507 550 ESQVsryKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEvsngHLVKRLEKMKANRSALL 613
Cdd:TIGR00606 418 QSKE---RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELK----FVIKELQQLEGSSDRIL 474
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
344-542 |
1.95e-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: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 344 ALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFF------DSVRSERDDLREEVVMLKEElkkh 417
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeidvASAEREIAELEAELERLDAS---- 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 418 giilNSEIATNGETSDTLnnvgyqgptkmtKEELNALKSTGDGtLDIRLKKLVDERECLLEQIKKLKGQLEERQKIGKL- 496
Cdd:COG4913 684 ----SDDLAALEEQLEEL------------EAELEELEEELDE-LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLe 746
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2462578507 497 DNLRSEDDVLENGTDMHVMDLQRDANRQISDLKFKLAKSEQEITAL 542
Cdd:COG4913 747 LRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
465-616 |
2.02e-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: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 465 RLKKLVDERECLLEQIKKLKGQLEE-----RQKIGKLDNLRSEDDVLEN------GTDMHVMDLQRDANRQISDLKFKLA 533
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEEltaelQELEEKLEELRLEVSELEEeieelqKELYALANEISRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 534 KSEQEITALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALL 613
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
...
gi 2462578507 614 SQQ 616
Cdd:TIGR02168 393 LQI 395
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
334-606 |
2.08e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 334 LQFQFAEVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEE 413
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 414 LKKHGIILnseiatnGETSDTLNNVgyqgptkmtKEELNALKST--------GDGTLDIRLKKLVDERECLLEQIKKLKG 485
Cdd:PRK03918 254 KRKLEEKI-------RELEERIEEL---------KKEIEELEEKvkelkelkEKAEEYIKLSEFYEEYLDELREIEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 486 QLEER-----QKIGKLDNLRSEDDVLENgtdmhvmdLQRDANRQISDLKfKLAKSEQEITALEQNVIRLESqvsryKSAA 560
Cdd:PRK03918 318 RLEEEingieERIKELEEKEERLEELKK--------KLKELEKRLEELE-ERHELYEEAKAKKEELERLKK-----RLTG 383
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2462578507 561 ENAEKIEDELK-AEKRK--LQRELRSALDKTEELEVSNGHLVKRLEKMK 606
Cdd:PRK03918 384 LTPEKLEKELEeLEKAKeeIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
337-416 |
2.86e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 40.44 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 337 QFAEVKEALKQR--EEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEEL 414
Cdd:PRK05431 10 NPEAVKEALAKRgfPLDVDELLELDEERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEVKELKEEIKALEAEL 89
|
..
gi 2462578507 415 KK 416
Cdd:PRK05431 90 DE 91
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
557-616 |
6.39e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 38.75 E-value: 6.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 557 KSAAENAEKIeDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMKANRSALLSQQ 616
Cdd:pfam11932 27 AAAAQSQKKI-DKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASLERQI 85
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
321-606 |
6.79e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.62 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 321 NKEFEREKHAHSILQFQFAEVKEALKQREE----MLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQK----EF 392
Cdd:TIGR04523 109 NSEIKNDKEQKNKLEVELNKLEKQKKENKKnidkFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKlniqKN 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 393 FDSVRSERDDLREEVVMLKEELKKHGiILNSEIATNGETSDTLNN---------VGYQGPTKMTKEELNALKSTGDgtld 463
Cdd:TIGR04523 189 IDKIKNKLLKLELLLSNLKKKIQKNK-SLESQISELKKQNNQLKDniekkqqeiNEKTTEISNTQTQLNQLKDEQN---- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 464 iRLKKLVDERECLLEQIKKLKGQLEERqkigkLDNLRSEDDVLEN----GTDMHVMDLQRDANRQISDLKFKLAKSEQEI 539
Cdd:TIGR04523 264 -KIKKQLSEKQKELEQNNKKIKELEKQ-----LNQLKSEISDLNNqkeqDWNKELKSELKNQEKKLEEIQNQISQNNKII 337
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462578507 540 TALEQNVIRLESQVSRYKSAAENAEKIEDELKAEKRKLQRELRSALDKTEELEVSNGHLVKRLEKMK 606
Cdd:TIGR04523 338 SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE 404
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
445-616 |
7.33e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 39.65 E-value: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 445 KMTKEELNALKSTGDGTLDIRLKKLVDEREcllEQIKKLKGQLEE--RQKIGKLDNLRSEDDVLEngtdmHVMDLQRDAN 522
Cdd:PRK10929 79 KLSAELRQQLNNERDEPRSVPPNMSTDALE---QEILQVSSQLLEksRQAQQEQDRAREISDSLS-----QLPQQQTEAR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 523 RQISDLKFKL--------AKSEQEITALEQNVIRLESQVSRYKSA--------------AENAEKIEDELKAEKRKL--- 577
Cdd:PRK10929 151 RQLNEIERRLqtlgtpntPLAQAQLTALQAESAALKALVDELELAqlsannrqelarlrSELAKKRSQQLDAYLQALrnq 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2462578507 578 -----QRELRSALDKTEELEVSNGHLVKRL-EKMKANR--SALLSQQ 616
Cdd:PRK10929 231 lnsqrQREAERALESTELLAEQSGDLPKSIvAQFKINRelSQALNQQ 277
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
348-585 |
8.11e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 348 REEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKEFFDSVRSERDDLREEVVMLKEELKKHGIILNSEiat 427
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL--- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 428 ngetsdtlnnvgyqgptkmtkeelnalkstgdgTLDIRLKKLVDERECLLEQIKKLKGQLEE-RQKIGKLDNLRSEDDVL 506
Cdd:COG4717 129 ---------------------------------PLYQELEALEAELAELPERLEELEERLEElRELEEELEELEAELAEL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462578507 507 ENGTDMHVMDLQRDANRQISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKiEDELKAEKRKLQRELRSAL 585
Cdd:COG4717 176 QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLL 253
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
257-592 |
9.81e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 38.85 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 257 TEASIREIKDSLAEVEEKYKKAMVSNAQLDNEKTNFMYQVDTLKDMLLELEEQLAESRRQYEEKNKEFEREKHAHSILQF 336
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 337 QfaeVKEALKQREEMLEEIRQLQQKQASSIREISDLQETIEWKDKKIGALERQKeffDSVRSERDDLREEVVMLKEELKK 416
Cdd:TIGR04523 413 Q---IKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTR---ESLETQLKVLSRSINKIKQNLEQ 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 417 hgiiLNSEIATNGETSDTLNNVGYQgptkmtkeelnalkstgdgtLDIRLKKLVDERECLLEQIKKLKgqLEERQKIGKL 496
Cdd:TIGR04523 487 ----KQKELKSKEKELKKLNEEKKE--------------------LEEKVKDLTKKISSLKEKIEKLE--SEKKEKESKI 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462578507 497 DNLRSEDDVLENGTDMHVMDLQRDANRQ--------ISDLKFKLAKSEQEITALEQNVIRLESQVSRYKSAAENAEKIED 568
Cdd:TIGR04523 541 SDLEDELNKDDFELKKENLEKEIDEKNKeieelkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELE 620
|
330 340
....*....|....*....|....
gi 2462578507 569 ELKAEKRKLQRELRSALDKTEELE 592
Cdd:TIGR04523 621 KAKKENEKLSSIIKNIKSKKNKLK 644
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|
| |
