|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
292-646 |
8.47e-103 |
|
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: 317.02 E-value: 8.47e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 292 LDEKSDKQYAENYT---------RPSSRNSASATTPLSGNSSRRGSGDTSSLIDPDTSLSELRDiydlkdqiqdvegrym 362
Cdd:pfam09738 30 VEENADRVFDMSSSsgadtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKH---------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 363 qglkelkeSLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKM 442
Cdd:pfam09738 94 --------ELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 443 EELKEGLRQRDELIeekqrmqqkidtmtkevfdlqetllwkdkkigalekqkeyiaclrnerdmlreeladlqetvktgE 522
Cdd:pfam09738 166 AELKEQLKQRDELI-----------------------------------------------------------------E 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 523 KHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQ-KCSRN 601
Cdd:pfam09738 181 KHGLVIVPDENTNGEEENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKSkRNSTR 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 530373301 602 DGTVGDLAGLQNGSDLqfIEMQRDANRQISEYKFKLSKAEQDITT 646
Cdd:pfam09738 261 SSQSPDGFGLENGSHV--IEVQREANKQISDYKFKLQKAEQEITT 303
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
322-697 |
1.25e-11 |
|
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: 68.17 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 322 NSSRRGSGDTSSliDPDTSLSELRDIYDLKDQ---IQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIY 398
Cdd:TIGR02169 660 RAPRGGILFSRS--EPAELQRLRERLEGLKRElssLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 399 QVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQrdELIEEKQRMQQKIDtmtKEVFDLQE 478
Cdd:TIGR02169 738 RLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLE---EEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 479 TLLWKDKKIGALEKQKEYiacLRNERDMLREELADLQETVKTGEKhglviipdgtpNGDVSHEPVAGAITVVSQEAAQVL 558
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEY---LEKEIQELQEQRIDLKEQIKSIEK-----------EIENLNGKKEELEEELEELEAALR 878
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 559 EsagegpLDVRLRKLAGEKEELLSQIRKLKL---QLEEERQKCSRNDGTVGDLAGLQNGsDLQFIEMQRDANRQISEYKF 635
Cdd:TIGR02169 879 D------LESRLGDLKKERDELEAQLRELERkieELEAQIEKKRKRLSELKAKLEALEE-ELSEIEDPKGEDEEIPEEEL 951
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530373301 636 KLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEME 697
Cdd:TIGR02169 952 SLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
365-696 |
5.22e-10 |
|
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: 63.15 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 365 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEE 444
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 445 LKEglrQRDELIEEKQRMQQKIDTMTKEVFDLQETLlwkDKKIGALEKQKEYIACLRNERDMLREELADLQETVKTGEKh 524
Cdd:TIGR02168 759 LEA---EIEELEERLEEAEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLESLER- 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 525 glviipdgtpngdvSHEPVAGAITVVSQEAAQVLEsagegpldvRLRKLAGEKEELLSQIRKLKLQLEE-ERQKCSRNDG 603
Cdd:TIGR02168 832 --------------RIAATERRLEDLEEQIEELSE---------DIESLAAEIEELEELIEELESELEAlLNERASLEEA 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 604 TVGDLAGLQN-GSDLQFIEMQR-DANRQISEYKFKLSKAEQDITTLEQSISRLEGQVL-RYKTAAENAEKVEDELKAEKR 680
Cdd:TIGR02168 889 LALLRSELEElSEELRELESKRsELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEE 968
|
330
....*....|....*.
gi 530373301 681 KLQRELRTALDKIEEM 696
Cdd:TIGR02168 969 EARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
326-696 |
6.63e-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: 59.30 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 326 RGSGDTSSLIdpdtsLSELRDIYDLKDQIQDVEGRYMQGLKELKESLSEVEEkYKKAMVSNAQLDNEKNNLIYQVDTLKD 405
Cdd:TIGR02168 663 GGSAKTNSSI-----LERRREIEELEEKIEELEEKIAELEKALAELRKELEE-LEEELEQLRKELEELSRQISALRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 406 VIEEQEEQMAEFYRENEEKSKELERQKhmcSVLQHKMEELKEGLrqrDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDK 485
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEI---EELEERLEEAEEEL---AEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 486 KIGALE----KQKEYIACLRNERDMLREELADLQETVKTGEKHGLVI---IPDGTPNGDVSHEPVAGAITVV-SQEAAQV 557
Cdd:TIGR02168 811 ELTLLNeeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEALLNERaSLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 558 LESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLagLQNGSDLQFIEMQrDANRQISEYKFKL 637
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL--QERLSEEYSLTLE-EAEALENKIEDDE 967
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 638 SKAEQDITTLEQSISRLeGQV-LRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEM 696
Cdd:TIGR02168 968 EEARRRLKRLENKIKEL-GPVnLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
352-697 |
2.30e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 352 DQIQDVegrymqgLKELKESL------SEVEEKYKkamvsnaQLDNEKNNLiyQVDTLKDVIEEQEEQMAEF---YRENE 422
Cdd:TIGR02168 189 DRLEDI-------LNELERQLkslerqAEKAERYK-------ELKAELREL--ELALLVLRLEELREELEELqeeLKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 423 EKSKELERQKHMcsvLQHKMEELKEGLRQRDELIEEKQR----MQQKIDTMTKEVFDLQETLLWKDKKIGALEkqkEYIA 498
Cdd:TIGR02168 253 EELEELTAELQE---LEEKLEELRLEVSELEEEIEELQKelyaLANEISRLEQQKQILRERLANLERQLEELE---AQLE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 499 CLRNERDMLREELADLQETVKTGEKhglviipdgtpngdvSHEPVAGAITvVSQEAAQVLESAGEGpLDVRLRKLAGEKE 578
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKE---------------ELESLEAELE-ELEAELEELESRLEE-LEEQLETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 579 ELLSQIRKLKLQLEEERQKCSRNDGTVGdlaglqngsdlQFIEMQRDANRQISEYKFKLSKAEqdITTLEQSISRLEGQV 658
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRE-----------RLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEEL 456
|
330 340 350
....*....|....*....|....*....|....*....
gi 530373301 659 LRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEME 697
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
419-668 |
8.40e-07 |
|
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: 51.69 E-value: 8.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 419 RENEEKSKELERQkhmcsvLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQkeyIA 498
Cdd:COG4942 23 AEAEAELEQLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE---IA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 499 CLRNERDMLREELAD-LQETVKTGEKHGL-VIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEgpldvRLRKLAGE 576
Cdd:COG4942 94 ELRAELEAQKEELAElLRALYRLGRQPPLaLLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----ELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 577 KEELLSQIRKLKLQLEEERQKcsrndgtvgdLAGLQNGSDlqfiEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEG 656
Cdd:COG4942 169 LEAERAELEALLAELEEERAA----------LEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
250
....*....|..
gi 530373301 657 QVLRYKTAAENA 668
Cdd:COG4942 235 EAAAAAERTPAA 246
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
348-523 |
4.09e-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: 50.44 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 348 YDLKDQIQDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKE 427
Cdd:TIGR02168 291 YALANEISRLEQQ----KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 428 LErqkhmcsVLQHKMEELKEGL-RQRDELIEEKQRMQQ---KIDTMTKEVFDLQETL---------LWKDKKIGALEKQK 494
Cdd:TIGR02168 367 LE-------ELESRLEELEEQLeTLRSKVAQLELQIASlnnEIERLEARLERLEDRRerlqqeieeLLKKLEEAELKELQ 439
|
170 180
....*....|....*....|....*....
gi 530373301 495 EYIACLRNERDMLREELADLQETVKTGEK 523
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELRE 468
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
399-712 |
4.68e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 4.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 399 QVDTLKDVIEEQEEQMAEFYRENEEKSKELErqkhmcsvLQHKMEELK--EGLRQRDELIEEKQRMQQKIDTMTKEVFDL 476
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLERLRREREKAERYQA--------LLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 477 QETLLWKDKKIGALEKQKEYIAclRNERDMLREELADLQETVktGEKHGLViipdgtpngdvshEPVAGAITVVSQEAAQ 556
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKI--GELEAEI-------------ASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 557 vlesagegpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNG--SDLQFIEMQRDANRQ-ISEY 633
Cdd:TIGR02169 320 ---------AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDlrAELEEVDKEFAETRDeLKDY 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530373301 634 KFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 712
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
351-614 |
5.56e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 351 KDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKN-------NLIYQVDTLKDVIEEQEEQMAEFYRENEE 423
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 424 KSKELERQKhmcSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQ----KEYIAC 499
Cdd:TIGR02168 321 LEAQLEELE---SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqlELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 500 LRNERDMLREELADLQETVktgEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEgpLDVRLRKLAGEKEE 579
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRR---ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELER--LEEALEELREELEE 472
|
250 260 270
....*....|....*....|....*....|....*
gi 530373301 580 LLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNG 614
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
403-721 |
5.61e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.94 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 403 LKDVIEEQEEQM---------AEFYRENEEKSKELERQkhmcsVLQHKMEELKEGLRQRDELIEEKQRMQQKIDtmtkev 473
Cdd:COG1196 191 LEDILGELERQLeplerqaekAERYRELKEELKELEAE-----LLLLKLRELEAELEELEAELEELEAELEELE------ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 474 fdlqetllwkdKKIGALEKQKEYiacLRNERDMLREELADLQEtvktgekhglviipdgtpngdvshepvagAITVVSQE 553
Cdd:COG1196 260 -----------AELAELEAELEE---LRLELEELELELEEAQA-----------------------------EEYELLAE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 554 AAQvlESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQkcsrndgtvgdlaglqngsdlqfiemqrdanrQISEY 633
Cdd:COG1196 297 LAR--LEQDIARLEERRRELEERLEELEEELAELEEELEELEE--------------------------------ELEEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 634 KFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKAN 713
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
....*...
gi 530373301 714 RTALLAQQ 721
Cdd:COG1196 423 LEELEEAL 430
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
349-712 |
5.62e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 349 DLKDQIQDVEGRYMQGLKELKESLSEVE---------EKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYR 419
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPelreeleklEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 420 ENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQEtllwkdkKIGALEKQKEYIAC 499
Cdd:PRK03918 270 ELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE-------RIKELEEKEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 500 LRNERDMLREELADLQETVKTGEKhglviipdgtpngdvshepvAGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEE 579
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEE--------------------AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 580 LLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQI-SEYKFKLSKAEQDITTLEQSISRL---- 654
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLrkel 482
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530373301 655 ---------EGQVLRYKTAAENAEKVEDELKA----EKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 712
Cdd:PRK03918 483 relekvlkkESELIKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
349-712 |
7.45e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 7.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 349 DLKDQIQDVE--------GRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEF 417
Cdd:PRK02224 191 QLKAQIEEKEekdlherlNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 418 YRENEEKSKELERQKHMCSVLqhkmEELKEGLRQRDELIE-EKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEy 496
Cdd:PRK02224 271 EREREELAEEVRDLRERLEEL----EEERDDLLAEAGLDDaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAE- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 497 iaCLRNERDMLREELADLQETVKTGEKhglviipdGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGPldVRLRKLAGE 576
Cdd:PRK02224 346 --SLREDADDLEERAEELREEAAELES--------ELEEAREAVEDRREEIEELEEEIEELRERFGDAP--VDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 577 KEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDL----QFIEMQRDANRqISEYKFKLSKAEQDITTLEQSIS 652
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgQPVEGSPHVET-IEEDRERVEELEAELEDLEEEVE 492
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530373301 653 RLEGQVLRYKTAAENAEKVEDelKAEKRKLQRELR-TALDKIEEMEMTNSHLAKRLEKMKA 712
Cdd:PRK02224 493 EVEERLERAEDLVEAEDRIER--LEERREDLEELIaERRETIEEKRERAEELRERAAELEA 551
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
345-720 |
1.10e-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: 48.90 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 345 RDIYDLKDQIQDVEgrymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQM-------AEF 417
Cdd:TIGR02168 316 RQLEELEAQLEELE----SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLetlrskvAQL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 418 YRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQR--MQQKIDTMTKEVFDLQETLlwkDKKIGALEKQKE 495
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEEL---ERLEEALEELRE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 496 YIACLRNERDMLREELA-----------------DLQETVKTGEKHGLVIIPDGTPNGD-VSHEP------------VAG 545
Cdd:TIGR02168 469 ELEEAEQALDAAERELAqlqarldslerlqenleGFSEGVKALLKNQSGLSGILGVLSElISVDEgyeaaieaalggRLQ 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 546 AITVVSQEAA----QVLESAGEG-----PLD-VRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAG----- 610
Cdd:TIGR02168 549 AVVVENLNAAkkaiAFLKQNELGrvtflPLDsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGgvlvv 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 611 --LQNGSDLQ--------FIEMQ--------------RDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAE 666
Cdd:TIGR02168 629 ddLDNALELAkklrpgyrIVTLDgdlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELE 708
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 530373301 667 NAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 720
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
566-720 |
1.18e-05 |
|
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: 47.23 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 566 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAglqngSDLQFIEMQ-RDANRQISEYKFKLSKA---- 640
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-----KEIKRLELEiEEVEARIKKYEEQLGNVrnnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 641 -----EQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEmtnSHLAKRLEKMKANRT 715
Cdd:COG1579 90 eyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAELEELEAERE 166
|
....*
gi 530373301 716 ALLAQ 720
Cdd:COG1579 167 ELAAK 171
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
343-714 |
1.40e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 343 ELRDIYDLKDQIQDVEGRymqgLKELKESLSEVEEK---YKKAMVSNAQLDNEKNNL-IYQVDTLKDVIEEQEEQMAEFY 418
Cdd:PRK03918 329 RIKELEEKEERLEELKKK----LKELEKRLEELEERhelYEEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 419 RENEEKSKELERQKHMCSVLQHKMEELKEGLRQ----RDELIEEKQrmQQKIDTMTKEVFDLQETLLWKDKKIGALEKQK 494
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 495 EYI-ACLRNERDMLR-EELAD-LQETVKTGEKHGLVIIPDGTPNGDVSHEPVAGaitvVSQEAAQVLESAGEG-PLDVRL 570
Cdd:PRK03918 483 RELeKVLKKESELIKlKELAEqLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK----LKGEIKSLKKELEKLeELKKKL 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 571 RKLAGEKEELLSQIRKLKLQLEEERQKCSRN-DGTVGDLAGLQNgsdlQFIEMqRDANRQISEYKFKLSKAEQDITTLEQ 649
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGFESVEElEERLKELEPFYN----EYLEL-KDAEKELEREEKELKKLEEELDKAFE 633
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 650 SISRLEGQVLRYKTAAENAEKVEDE-----LKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANR 714
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
346-717 |
1.58e-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: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 346 DIYDLKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEK---NNLIYQVDTLKDVIEEQEEQMAEFYRENE 422
Cdd:TIGR04523 69 KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKeqkNKLEVELNKLEKQKKENKKNIDKFLTEIK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 423 EKSKELERQKHMCSVLQHKMEELKEglrQRDELIEEKQRMQQKIDTMTKEVFDLQETLL---WKDKKIGALEKQ----KE 495
Cdd:TIGR04523 149 KKEKELEKLNNKYNDLKKQKEELEN---ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSnlkKKIQKNKSLESQiselKK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 496 YIACLRNERDMLREELADLQETVKTGEKHGLVIIPDGTPNGDVSHEP---VAGAITVVSQEAAQVLEsagegpLDVRLRK 572
Cdd:TIGR04523 226 QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKqkeLEQNNKKIKELEKQLNQ------LKSEISD 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 573 LAGEKE-----ELLSQIRKLKLQLEEERQKCSRNDGTVGDLaglqnGSDLQFIEMQRD--------ANRQISEYKFKLSK 639
Cdd:TIGR04523 300 LNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQL-----NEQISQLKKELTnsesenseKQRELEEKQNEIEK 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530373301 640 AEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTAL 717
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
341-717 |
1.72e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 341 LSELRDIYDLKDQIQDVEGRYmqglKELKESLSEVEEKYKKAMVSNAQLDNEKNNLiyqvdtlkdvieEQEEQMAEFYRE 420
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKL------------EKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 421 NEEKSKELERqkhmcsvLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKigALEKQKEYIACL 500
Cdd:COG4717 134 LEALEAELAE-------LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE--ELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 501 RNERDMLREELADLQETVKTGEKH----------------------------GLVIIPDGTPNGDVSHEPVAGAITVV-- 550
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEEleqleneleaaaleerlkearlllliaaALLALLGLGGSLLSLILTIAGVLFLVlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 551 ---------SQEAAQVLESAGEGPLDVRLRKLAGEK-------------------EELLSQIRKLKL------QLEEERQ 596
Cdd:COG4717 285 llallflllAREKASLGKEAEELQALPALEELEEEEleellaalglppdlspeelLELLDRIEELQEllreaeELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 597 KCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQIsEYKFKLSKAEQDITTLEQSI---------SRLEGQVLRYKTAAEN 667
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELeellealdeEELEEELEELEEELEE 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 530373301 668 AEKVEDELKAEKRKLQRELRT---------ALDKIEEMEMTNSHLAKRLEKMKANRTAL 717
Cdd:COG4717 444 LEEELEELREELAELEAELEQleedgelaeLLQELEELKAELRELAEEWAALKLALELL 502
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
346-565 |
1.78e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 346 DIYDLKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEFYRENE 422
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEalqAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 423 EKSKE----------------LERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETllwKDKK 486
Cdd:COG3883 97 RSGGSvsyldvllgsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA---KAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530373301 487 IGALEKQKEYIACLRNERDMLREELADLQETVKTGEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGP 565
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
415-698 |
1.83e-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: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 415 AEFYRENEEKSKELERQKHMCSVLQHKMEELKEglrQRDELIEEKQRmQQKIDTMTKEVFDLQETLLWKDKKigALEKQK 494
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREK-AERYQALLKEKREYEGYELLKEKE--ALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 495 EYIaclRNERDMLREELADLQETVKTGEKHglviipdgtpngdvshepVAGAITVVSQEAAQVLESAGEGPLDVR--LRK 572
Cdd:TIGR02169 240 EAI---ERQLASLEEELEKLTEEISELEKR------------------LEEIEQLLEELNKKIKDLGEEEQLRVKekIGE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 573 LAGEKEELLSQIRKLKLQLE----EERQKCSRNDGTVGDLAGLQngSDLQFIEMQRDA-NRQISEYKFKLSKAEQDITTL 647
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEdaeeRLAKLEAEIDKLLAEIEELE--REIEEERKRRDKlTEEYAELKEELEDLRAELEEV 376
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 530373301 648 EQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEM 698
Cdd:TIGR02169 377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
350-721 |
2.26e-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: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 350 LKDQIQDVEGRYMQGL-KELKESLSEVEEKYKkamvsnaQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 428
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWnKELKSELKNQEKKLE-------EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 429 ERqkhmcsvlqhKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEYiacLRNERDMLR 508
Cdd:TIGR04523 366 EE----------KQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL---LEKEIERLK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 509 EELADLQETVKTGEKhglviipdgtpngdvshepvagaitvvsQEAAqvlesagegpLDVRLRKLAGEKEELLSQIRKLK 588
Cdd:TIGR04523 433 ETIIKNNSEIKDLTN----------------------------QDSV----------KELIIKNLDNTRESLETQLKVLS 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 589 LQLEEERQKCSRNdgtvgdlaglqngsdlqfiemqrdanrqiseyKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENA 668
Cdd:TIGR04523 475 RSINKIKQNLEQK--------------------------------QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSL 522
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530373301 669 EKVEDELKAEKRKLQRELRTALDKIEEMEMTN---------SHLAKRLEKMKANRTALLAQQ 721
Cdd:TIGR04523 523 KEKIEKLESEKKEKESKISDLEDELNKDDFELkkenlekeiDEKNKEIEELKQTQKSLKKKQ 584
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
499-721 |
3.10e-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: 47.36 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 499 CLRNERDMLREELADLQETVKTGEKhglviipdgtpngdvshepvagAITVVSQEAAQVLEsagegpldvRLRKLAGEKE 578
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEK----------------------ALAELRKELEELEE---------ELEQLRKELE 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 579 ELLSQIRKLKLQLEEERQKCSRndgtVGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQV 658
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530373301 659 LRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 721
Cdd:TIGR02168 799 KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
349-523 |
3.58e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.81 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 349 DLKDQIQDVEgrymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 428
Cdd:pfam07888 77 ELESRVAELK----EELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 429 ERQKhmcsvlqhkmEELKEGLRQRDELIEEKQRMQQKIDTMTKEV----FDLQETLLWKDKKIGALEKQKEYIACLRN-- 502
Cdd:pfam07888 153 ERMK----------ERAKKAGAQRKEEEAERKQLQAKLQQTEEELrslsKEFQELRNSLAQRDTQVLQLQDTITTLTQkl 222
|
170 180
....*....|....*....|....*....
gi 530373301 503 --------ERDMLREELADLQETVKTGEK 523
Cdd:pfam07888 223 ttahrkeaENEALLEELRSLQERLNASER 251
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
349-697 |
4.04e-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: 46.94 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 349 DLKDQIQDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 428
Cdd:TIGR04523 311 ELKSELKNQEKK----LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 429 ERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDtmtKEVFDLQETLLWKDKKIGALEKQ----KEYIACLRNER 504
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE---KEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTR 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 505 DMLREELADLQETVKTgEKHGLviipdgtpngdvshEPVAGAITVVSQEAAQVLESAGEgpLDVRLRKLAGEKEELLSQI 584
Cdd:TIGR04523 464 ESLETQLKVLSRSINK-IKQNL--------------EQKQKELKSKEKELKKLNEEKKE--LEEKVKDLTKKISSLKEKI 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 585 RKLKLQLEEERQKCSRNDgtvGDLAGLQNGSDLQFIEMQRDA-NRQISEYKF-------KLSKAEQDITTLEQSISRLEG 656
Cdd:TIGR04523 527 EKLESEKKEKESKISDLE---DELNKDDFELKKENLEKEIDEkNKEIEELKQtqkslkkKQEEKQELIDQKEKEKKDLIK 603
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 530373301 657 QVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEME 697
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
363-704 |
5.54e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.74 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 363 QGLKELKESLSEVEEKykkamvsnaqldneKNNLIYQVDTLKDVIEEQEEQMAE----FYRENEEKSK---ELERQKHM- 434
Cdd:pfam10174 324 QHIEVLKESLTAKEQR--------------AAILQTEVDALRLRLEEKESFLNKktkqLQDLTEEKSTlagEIRDLKDMl 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 435 ------CSVLQHKMEELKEGLRQRDELIEEKQR----MQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEYI-ACLRNE 503
Cdd:pfam10174 390 dvkerkINVLQKKIENLQEQLRDKDKQLAGLKErvksLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREdRERLEE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 504 RDMLREELADLQETVKTGEKHGL----VIIPDGTPNGDVSHEPVAGAITVVSQEAAqvLESAGEGP--LDVRLRKL---- 573
Cdd:pfam10174 470 LESLKKENKDLKEKVSALQPELTekesSLIDLKEHASSLASSGLKKDSKLKSLEIA--VEQKKEECskLENQLKKAhnae 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 574 --AGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGL-------QNGSDLQFIEMQRDANRQISEykfkLSKAEQDI 644
Cdd:pfam10174 548 eaVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGIlreveneKNDKDKKIAELESLTLRQMKE----QNKKVANI 623
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530373301 645 TTLEQSISRLEGQVLryktaaENAEKVEDELKAEKRKLQ-RELRTALDKI-EEMEMTNSHLA 704
Cdd:pfam10174 624 KHGQQEMKKKGAQLL------EEARRREDNLADNSQQLQlEELMGALEKTrQELDATKARLS 679
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
407-717 |
5.67e-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: 46.60 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 407 IEEQEEQMAEFYRENEEKSKELER------QKHMCSVLQHKMEELK--EGLRQRDELIEEKQRMQQKIDTMTKEVFDLQE 478
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERlrrereKAERYQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKLTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 479 TLLWKDKKIGALEKQKEYIAclRNERDMLREELADLQETVK--TGEKHGLV-IIPDGTPNGDVSHEPVAGAITVVSQEAA 555
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKIGelEAEIASLErSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 556 QVLESAGE-GPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKcsrNDGTVGDLAGLQNGSDlQFIEMQRDANRQISEYK 634
Cdd:TIGR02169 337 EIEELEREiEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE---FAETRDELKDYREKLE-KLKREINELKRELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 635 FKLSKAEQDITTLEQSISRLEGQVLRYKTAAENA----EKVEDELK---AEKRKLQRELRTALDKIEEMEMTNSHLAKRL 707
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKaleiKKQEWKLEqlaADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
330
....*....|
gi 530373301 708 EKMKANRTAL 717
Cdd:TIGR02169 493 AEAEAQARAS 502
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
566-712 |
6.55e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 566 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCsrnDGTVGDLAGlQNGSDLQFIEMQ-RDANRQISEYKFKLSKAEQDI 644
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREEL---DELEAQIRG-NGGDRLEQLEREiERLERELEERERRRARLEALL 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530373301 645 TTLEQSI-----------SRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 712
Cdd:COG4913 369 AALGLPLpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
346-695 |
6.80e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 346 DIYDLKDQIQDVEGRymqgLKELKESLSEVEE--KYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEE 423
Cdd:PRK03918 260 KIRELEERIEELKKE----IEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 424 KSKELERQKHMCSVLQHKMEELKEGLRQRDE---LIEEKQRMQQKIDTMTKEVFdlqetllwkDKKIGALEKQKEYIacl 500
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELYEEakaKKEELERLKKRLTGLTPEKL---------EKELEELEKAKEEI--- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 501 RNERDMLREELADLQETVKTGEKhglVIIPDGTPNGDVshePVAGAiTVVSQEAAQVLESAGEGPLDVR--LRKLAGEKE 578
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKK---AIEELKKAKGKC---PVCGR-ELTEEHRKELLEEYTAELKRIEkeLKEIEEKER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 579 ELLSQIRKLKLQLEEERqKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQV 658
Cdd:PRK03918 477 KLRKELRELEKVLKKES-ELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELK 555
|
330 340 350
....*....|....*....|....*....|....*..
gi 530373301 659 LRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEE 695
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELEELGFESVEELEE 592
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
554-721 |
7.98e-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: 46.20 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 554 AAQVLESAGEG--PLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNgsdlQFIEMQRDANRQIS 631
Cdd:TIGR02168 230 LVLRLEELREEleELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY----ALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 632 EYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMK 711
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170
....*....|
gi 530373301 712 ANRTALLAQQ 721
Cdd:TIGR02168 386 SKVAQLELQI 395
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
372-710 |
9.65e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 372 LSEVEEKYKKAMVSNAQLDNEKNNL---IYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEG 448
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 449 LRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQ-----------KEYIAcLRNERDMLREELADLQET 517
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkelkekaEEYIK-LSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 518 vktgekhglviipdgtpngdvshepvagaITVVSQEAAQVLESAGEGPLDV-RLRKLAGEKEELLSQIRKLK---LQLEE 593
Cdd:PRK03918 316 -----------------------------LSRLEEEINGIEERIKELEEKEeRLEELKKKLKELEKRLEELEerhELYEE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 594 ERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQISEykfKLSKAEQDITTLEQSISRLEGQVLRYKTAAE-----NA 668
Cdd:PRK03918 367 AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEE---EISKITARIGELKKEIKELKKAIEELKKAKGkcpvcGR 443
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 530373301 669 EKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKM 710
Cdd:PRK03918 444 ELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
490-717 |
1.40e-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: 45.43 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 490 LEKQKEYIACLRNERDMLREELADLQETVKTGEKHGLviipdgtpngDVSHEPVAGAITVVSQEAAQVLESAGEGPLDVR 569
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELE----------ELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 570 LRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQ----------ISEYKFKLSK 639
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeaanlrerLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 640 AEQDITTLEQSISRLEGQVLRY----KTAAENAEKVEDELKA---EKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 712
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLaaeiEELEELIEELESELEAllnERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
....*
gi 530373301 713 NRTAL 717
Cdd:TIGR02168 916 ELEEL 920
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
365-691 |
1.51e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 365 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQM----AEFYRENEEKSKELERQKHMCSVLQH 440
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 441 KMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLlwKDKKIGALEKQKEYIACLRNERDMLREELADLQEtvkt 520
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL--AEAEEALLEAEAELAEAEEELEELAEELLEALRA---- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 521 gekhglviipdgtpngdvshepvagaitvVSQEAAQVLEsagegpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSR 600
Cdd:COG1196 395 -----------------------------AAELAAQLEE------LEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 601 NDGTVGDLAGLQNGSDLQfiemQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAE-KVEDELKAEK 679
Cdd:COG1196 440 EEEALEEAAEEEAELEEE----EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALL 515
|
330
....*....|..
gi 530373301 680 RKLQRELRTALD 691
Cdd:COG1196 516 LAGLRGLAGAVA 527
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
365-714 |
1.69e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 365 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVI------------EEQEEQMAEFYRENEEKSKELERQK 432
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteEHRKELLEEYTAELKRIEKELKEIE 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 433 HMCSVLQHKMEELKEGLRQRDELIEEKQRMQQ--------------KIDTMTKEVFDLQETLLWKDKKIGALEKQKEYIA 498
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESELIKLKELAEQlkeleeklkkynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 499 CLRNERDMLREELADLQETVKTGEKHGLVIipdgtpnGDVSHEPVAGAItvvsqeaaQVLESAGEGPLdvRLRKLAGEKE 578
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEEL-------GFESVEELEERL--------KELEPFYNEYL--ELKDAEKELE 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 579 ELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNgsdlqfiemqrDANRQISEYKFKlsKAEQDITTLEQSISRLEGQV 658
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELE-----------ELEKKYSEEEYE--ELREEYLELSRELAGLRAEL 682
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 530373301 659 lryktaaENAEKVEDELKAEKRKLQRELRTALDKIEEMEMtnshLAKRLEKMKANR 714
Cdd:PRK03918 683 -------EELEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
353-708 |
1.91e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 353 QIQDVEGRYMQGLKELKESLsEVEEKYKKAMVSNAQ-LDNEKNNLIYQVDTLkdvieEQEEQmaefyrENEEKSKELERQ 431
Cdd:pfam01576 346 QLQEMRQKHTQALEELTEQL-EQAKRNKANLEKAKQaLESENAELQAELRTL-----QQAKQ------DSEHKRKKLEGQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 432 khmcsvLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKE---------------- 495
Cdd:pfam01576 414 ------LQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQdtqellqeetrqklnl 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 496 --YIACLRNERDMLREELADLQETVKTGEKHGLviipdgtpngdvSHEPVAGAITVVSQEAAQVLESAGEGpldvrlrkl 573
Cdd:pfam01576 488 stRLRQLEDERNSLQEQLEEEEEAKRNVERQLS------------TLQAQLSDMKKKLEEDAGTLEALEEG--------- 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 574 ageKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGlqngsDLQFIEMQRDANRQIseykfkLSKAEQDITTLEQSISR 653
Cdd:pfam01576 547 ---KKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ-----ELDDLLVDLDHQRQL------VSNLEKKQKKFDQMLAE 612
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 530373301 654 LEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLE 708
Cdd:pfam01576 613 EKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEME 667
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
349-520 |
1.97e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 349 DLKDQIQDVEGRY---MQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKS 425
Cdd:TIGR04523 465 SLETQLKVLSRSInkiKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 426 KELERQK------HMCSVLQHKMEELKEgLRQRDELIEEKQR-MQQKIDTMTKEVFDLQETLLWKDKKIGALEKQ----- 493
Cdd:TIGR04523 545 DELNKDDfelkkeNLEKEIDEKNKEIEE-LKQTQKSLKKKQEeKQELIDQKEKEKKDLIKEIEEKEKKISSLEKElekak 623
|
170 180 190
....*....|....*....|....*....|...
gi 530373301 494 KEY------IACLRNERDMLREELADLQETVKT 520
Cdd:TIGR04523 624 KENeklssiIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
451-720 |
2.32e-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: 43.98 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 451 QRDELIEEKQRMQQKIDTMTKEVFDLQETllwKDKKIGALEKQKEYIACLRNERDMLREELADLQEtvktgekhglviip 530
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKE---EKALLKQLAALERRIAALARRIRALEQELAALEA-------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 531 dgtpngdvshepvagaitvvsqeaaqvlesagegpldvRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNdGTVGDLAG 610
Cdd:COG4942 84 --------------------------------------ELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLAL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 611 LQNGSDLQFIEMQRDANRQISEYKfklskaEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTAL 690
Cdd:COG4942 125 LLSPEDFLDAVRRLQYLKYLAPAR------REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ 198
|
250 260 270
....*....|....*....|....*....|
gi 530373301 691 DKIEEMEMTNSHLAKRLEKMKANRTALLAQ 720
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
416-711 |
2.83e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 416 EFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETllwkDKKIGALEKQKE 495
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL----KEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 496 YiacLRNERDMLREELADLQETVKTGEKHglviipdgtpngdvshepvagaITVVSQEAAQVLESAGEGPLDVRLRKLAG 575
Cdd:PRK03918 249 S---LEGSKRKLEEKIRELEERIEELKKE----------------------IEELEEKVKELKELKEKAEEYIKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 576 EKEELLSQIRKLKLQLEEERQKCSRNdgtvgdlaglqngsdlqfIEMQRDANRQISEYKFKLSKAEQDITTLE------Q 649
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEER------------------IKELEEKEERLEELKKKLKELEKRLEELEerhelyE 365
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530373301 650 SISRLEGQVLRYKT--AAENAEKVEDELK-AEKRK--LQRELRTALDKIEEMEMTNSHLAKRLEKMK 711
Cdd:PRK03918 366 EAKAKKEELERLKKrlTGLTPEKLEKELEeLEKAKeeIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
341-473 |
3.03e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 341 LSELRDIYD-LKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQ-----VDTLKDVIEEQEEQM 414
Cdd:COG1579 33 LAELEDELAaLEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEalqkeIESLKRRISDLEDEI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 415 AEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQR-DELIEEKQRMQQKIDTMTKEV 473
Cdd:COG1579 113 LELMERIEELEEELAELEAELAELEAELEEKKAELDEElAELEAELEELEAEREELAAKI 172
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
365-717 |
5.03e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 365 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQH---K 441
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvqtE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 442 MEELKEGLRQRDELIEekqRMQQKIDTMTKEVFDLQETllwkdkkIGALEKQKEYIACLRNERDMLREELADLQET--VK 519
Cdd:pfam15921 550 CEALKLQMAEKDKVIE---ILRQQIENMTQLVGQHGRT-------AGAMQVEKAQLEKEINDRRLELQEFKILKDKkdAK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 520 TGEKHGLViipdgtpnGDVSHEPV----AG-----AITVVSQEAAQVLESAGEG---------PLDVRLRKLAGEKEELL 581
Cdd:pfam15921 620 IRELEARV--------SDLELEKVklvnAGserlrAVKDIKQERDQLLNEVKTSrnelnslseDYEVLKRNFRNKSEEME 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 582 SQIRKLKLQLEEERQKCSRNDGTVGDLaglqNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISrlegqvlry 661
Cdd:pfam15921 692 TTTNKLKMQLKSAQSELEQTRNTLKSM----EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMT--------- 758
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 662 ktaaeNAEKVEDELKAEKRKLQRELRT-ALDKIE---EMEMTNSHLAKRLEKMKANRTAL 717
Cdd:pfam15921 759 -----NANKEKHFLKEEKNKLSQELSTvATEKNKmagELEVLRSQERRLKEKVANMEVAL 813
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
338-710 |
6.44e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 338 DTSLSEL-RDIYDLKDQIQDVEGRYMQGLKELKESLSEVE--EKYKKAMVSNA-QLDNEKNNLIYQVDTLKDVIEEQEEQ 413
Cdd:pfam10174 239 DTKISSLeRNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEvyKSHSKFMKNKIdQLKQELSKKESELLALQTKLETLTNQ 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 414 MAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEK----QRMQQKIDTMTKEVFDLQETLLWKDKKIGA 489
Cdd:pfam10174 319 NSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKtkqlQDLTEEKSTLAGEIRDLKDMLDVKERKINV 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 490 LEKQKEyiaclrNERDMLRE---ELADLQETVKTGEKHglviipdgTPNGDVSHEPVAGAITvvsqEAAQVLEsagegpl 566
Cdd:pfam10174 399 LQKKIE------NLQEQLRDkdkQLAGLKERVKSLQTD--------SSNTDTALTTLEEALS----EKERIIE------- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 567 dvRLRK-LAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDlaglQNGSdlqFIEMQRDANRQISEYKFKLSKAEQDIT 645
Cdd:pfam10174 454 --RLKEqREREDRERLEELESLKKENKDLKEKVSALQPELTE----KESS---LIDLKEHASSLASSGLKKDSKLKSLEI 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 646 TLEQSI---SRLEGQVLRYKTAAENAEKVED-------------ELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEK 709
Cdd:pfam10174 525 AVEQKKeecSKLENQLKKAHNAEEAVRTNPEindrirlleqevaRYKEESGKAQAEVERLLGILREVENEKNDKDKKIAE 604
|
.
gi 530373301 710 M 710
Cdd:pfam10174 605 L 605
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
345-523 |
6.58e-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: 43.13 E-value: 6.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 345 RDIYDLKDQIQDVEGRYMQGLKELKESLSEVEE---KYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYREN 421
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEElerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 422 EEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEkqrMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEYIAclr 501
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELAD---LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA--- 461
|
170 180
....*....|....*....|..
gi 530373301 502 NERDMLREELADLQETVKTGEK 523
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEK 483
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
397-591 |
8.57e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 397 IYQVDTLK--DVI---EEQEEQMAEFYRENEEKSKELERQKhmcSVLQHKMEELKEglrQRDELIEE-KQRMQQKIDTMT 470
Cdd:PRK00409 510 LIGEDKEKlnELIaslEELERELEQKAEEAEALLKEAEKLK---EELEEKKEKLQE---EEDKLLEEaEKEAQQAIKEAK 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 471 KEVFDLQETLLWKDKKIGALEKQKEYIACLR--NERDMLREELADL----QETVKTGEKhglVIIPDGTPNGDVshepva 544
Cdd:PRK00409 584 KEADEIIKELRQLQKGGYASVKAHELIEARKrlNKANEKKEKKKKKqkekQEELKVGDE---VKYLSLGQKGEV------ 654
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 530373301 545 gaITVVSQEAAQVLesagEGPLDVR-----LRKLAGEKEELLSQIRKLKLQL 591
Cdd:PRK00409 655 --LSIPDDKEAIVQ----AGIMKMKvplsdLEKIQKPKKKKKKKPKTVKPKP 700
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
621-712 |
8.86e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 621 EMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKtaAENA-------------EKVEDELKAEKRKLQRELR 687
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE--AEVEeleaeleekderiERLERELSEARSEERREIR 462
|
90 100 110
....*....|....*....|....*....|....*...
gi 530373301 688 -----TALD--------KIEEMEMTNSHLAKRLEKMKA 712
Cdd:COG2433 463 kdreiSRLDreierlerELEEERERIEELKRKLERLKE 500
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
388-711 |
9.53e-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: 42.80 E-value: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 388 QLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSvlqhkmEELKEGLRQRDELIEEKQRMQqkiD 467
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN------SELTEARTERDQFSQESGNLD---D 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 468 TMTKEVFDLQetllwKDKKIGALEKQKEYIACLRNER-----DMLREELADLQETVKTGEkhGLVIIPDGTPNGDVSHEP 542
Cdd:pfam15921 378 QLQKLLADLH-----KREKELSLEKEQNKRLWDRDTGnsitiDHLRRELDDRNMEVQRLE--ALLKAMKSECQGQMERQM 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 543 VA-----GAITVVSQEAAQvLESAGEGPLDVrLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDL 617
Cdd:pfam15921 451 AAiqgknESLEKVSSLTAQ-LESTKEMLRKV-VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 618 QFIEMQ---------RDANRQISEYKFKLSKAEQDITTLEQSI---SRLEGQVLRyKTAAENAEKVEDELKAEKRKLQ-R 684
Cdd:pfam15921 529 KLQELQhlknegdhlRNVQTECEALKLQMAEKDKVIEILRQQIenmTQLVGQHGR-TAGAMQVEKAQLEKEINDRRLElQ 607
|
330 340 350
....*....|....*....|....*....|.
gi 530373301 685 ELRTALD----KIEEMEMTNSHLakRLEKMK 711
Cdd:pfam15921 608 EFKILKDkkdaKIRELEARVSDL--ELEKVK 636
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
365-698 |
1.02e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 365 LKELKESLSEVEEKYKKamvsnaqldnEKNNLIYQVDTLKDVIEEQEEQMAEF---YRENEEKSKELERQKHMCSvlqhk 441
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKK----------EINDKEKQVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQD----- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 442 mEELKEGLRQRDELIEE----KQRMQQKIDTMTKevfdLQETLLWKDKKIGALEKQKEyiaclrnerdmlreelADLQET 517
Cdd:pfam05483 282 -ENLKELIEKKDHLTKElediKMSLQRSMSTQKA----LEEDLQIATKTICQLTEEKE----------------AQMEEL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 518 VKTGEKHGLVIipdgtpngdVSHEPVAGAITVVSQEAAQVLESAGE--GPLDVRLRKLAGEKEELLSQIRKLKLQLEE-- 593
Cdd:pfam05483 341 NKAKAAHSFVV---------TEFEATTCSLEELLRTEQQRLEKNEDqlKIITMELQKKSSELEEMTKFKNNKEVELEElk 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 594 ----ERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKaeqdITTLEQSISRlegQVLRYKTAAENAE 669
Cdd:pfam05483 412 kilaEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTA----IKTSEEHYLK---EVEDLKTELEKEK 484
|
330 340
....*....|....*....|....*....
gi 530373301 670 KVEDELKAEKRKLQRELRTALDKIEEMEM 698
Cdd:pfam05483 485 LKNIELTAHCDKLLLENKELTQEASDMTL 513
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
338-684 |
1.10e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 338 DTSLSELRDIYDLKDQIQDVEGRY---MQGLKELKESLSEVEEKYKKAmvsNAQLDNEKNNLIYQvdtlkdvieEQEEQm 414
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDYQAA---SDHLNLVQTALRQQ---------EKIER- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 415 aefYREN-EEKSKELERQkhmcsvlqhkMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIG----- 488
Cdd:PRK04863 353 ---YQADlEELEERLEEQ----------NEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIqyqqa 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 489 --ALEKQK--------------EYIACLRNERDMLREELADLQETVKtgekhglviipdgtpngdvshepvagaitvVSQ 552
Cdd:PRK04863 420 vqALERAKqlcglpdltadnaeDWLEEFQAKEQEATEELLSLEQKLS------------------------------VAQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 553 EAAQVLESAGEgpldvRLRKLAGE--KEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQngsdlQFIEMQRDANRQI 630
Cdd:PRK04863 470 AAHSQFEQAYQ-----LVRKIAGEvsRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELE-----QRLRQQQRAERLL 539
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 530373301 631 SEYKFKLSKAEQDITTLEQSISRLEGQVLRYK----TAAENAEKVEDELKAEKRKLQR 684
Cdd:PRK04863 540 AEFCKRLGKNLDDEDELEQLQEELEARLESLSesvsEARERRMALRQQLEQLQARIQR 597
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
407-712 |
1.15e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.40 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 407 IEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKK 486
Cdd:pfam05483 372 LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 487 IGALEKQkeyIACLRNERDMLREELADLQETVKtgekhglviipdgtpNGDVSHEPVAGAITVVSQEAAQVLESAGEGPL 566
Cdd:pfam05483 452 IHDLEIQ---LTAIKTSEEHYLKEVEDLKTELE---------------KEKLKNIELTAHCDKLLLENKELTQEASDMTL 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 567 DVR-----LRKLAGEKEELLSQIRKLK---LQLEEERQKCSRNDGTVGDLAGL------QNGSDLQFIEMQRDANRQISE 632
Cdd:pfam05483 514 ELKkhqedIINCKKQEERMLKQIENLEekeMNLRDELESVREEFIQKGDEVKCkldkseENARSIEYEVLKKEKQMKILE 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 633 YkfKLSKAEQDITTLEQSISRL--EGQVLRYKTAAENAE---------KVEDELKAEKRKLQRELRTALDKIEEMEMTNS 701
Cdd:pfam05483 594 N--KCNNLKKQIENKNKNIEELhqENKALKKKGSAENKQlnayeikvnKLELELASAKQKFEEIIDNYQKEIEDKKISEE 671
|
330
....*....|.
gi 530373301 702 HLAKRLEKMKA 712
Cdd:pfam05483 672 KLLEEVEKAKA 682
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
397-703 |
1.74e-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: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 397 IYQVDTLKDVIEEQEEQMAE------FYRENEEKSKELERQkhmCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMT 470
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEhqmelkYLKQYKEKACEIRDQ---ITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 471 KEVFDLQETllwkdkkIGALEKQKEyiaclrnERDMLREELADLQETVKTGEKHGLviipdgtpnGDVSHEPVAgaiTVV 550
Cdd:TIGR00606 262 SKIMKLDNE-------IKALKSRKK-------QMEKDNSELELKMEKVFQGTDEQL---------NDLYHNHQR---TVR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 551 SQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDlagLQNGSDLQFIEMQRDANRQI 630
Cdd:TIGR00606 316 EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS---LATRLELDGFERGPFSERQI 392
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530373301 631 SEY-KFKLSKAEQDITTLEQSISRLEGQVlryKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHL 703
Cdd:TIGR00606 393 KNFhTLVIERQEDEAKTAAQLCADLQSKE---RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL 463
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
343-717 |
1.80e-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: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 343 ELRDIYDLKDQIQDVEGRyMQGLKELKESLSEVEEKYKKAMvSNAQLDNEKNNLIY----QVDTLKDVIEEQEEqmaefy 418
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGS-SDRILELDQELRKAERELSKAE-KNSLTETLKKEVKSlqneKADLDRKLRKLDQE------ 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 419 reNEEKSKELERQKHMCSVLQHKMEE----LKEGLRQRDELIEE------KQRMQQKIDTMTKEVFDLQETLLWKDKKIG 488
Cdd:TIGR00606 524 --MEQLNHHTTTRTQMEMLTKDKMDKdeqiRKIKSRHSDELTSLlgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELA 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 489 ALEKQKEYIaclRNERDMLREELADLQETV-----KTGEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVL-ESAG 562
Cdd:TIGR00606 602 SLEQNKNHI---NNELESKEEQLSSYEDKLfdvcgSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTdENQS 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 563 EGPLDVRLRKLAGEKEELLSQIR--------KLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQ------RDANR 628
Cdd:TIGR00606 679 CCPVCQRVFQTEAELQEFISDLQsklrlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPelrnklQKVNR 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 629 QISEYKFKLSKAEQ-----------------DITTLEQSISRLEGQVLRYKTAAENAEKVE-----DELKAEKRKLQREL 686
Cdd:TIGR00606 759 DIQRLKNDIEEQETllgtimpeeesakvcltDVTIMERFQMELKDVERKIAQQAAKLQGSDldrtvQQVNQEKQEKQHEL 838
|
410 420 430
....*....|....*....|....*....|.
gi 530373301 687 RTALDKIEEMEMTNSHLAKRLEKMKANRTAL 717
Cdd:TIGR00606 839 DTVVSKIELNRKLIQDQQEQIQHLKSKTNEL 869
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
342-523 |
1.98e-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: 41.54 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 342 SELRDIYDLKDQIQDVEGRYM----------QGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQ-------VDTLK 404
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQnqeklnqqkdEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkeliIKNLD 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 405 DVIEEQEEQMAEFYRE-------NEEKSKELERQKHMCSVLQHKMEELKEGL----RQRDELIE-------EKQRMQQKI 466
Cdd:TIGR04523 461 NTRESLETQLKVLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVkdltKKISSLKEkieklesEKKEKESKI 540
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 530373301 467 DTMTKEVFDLQETLLWKDKKIGALEKQKEyIACLRNERDMLREELADLQETVKTGEK 523
Cdd:TIGR04523 541 SDLEDELNKDDFELKKENLEKEIDEKNKE-IEELKQTQKSLKKKQEEKQELIDQKEK 596
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
349-516 |
2.05e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 349 DLKDQIQDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 428
Cdd:COG4942 24 EAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 429 ERQKHMCSVL------QHKMEELKEGLRQRD--ELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEYIACL 500
Cdd:COG4942 100 EAQKEELAELlralyrLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170
....*....|....*.
gi 530373301 501 RNERDMLREELADLQE 516
Cdd:COG4942 180 LAELEEERAALEALKA 195
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
365-691 |
2.07e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 365 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLiyqvdtlkdviEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKME- 443
Cdd:pfam01576 14 LQKVKERQQKAESELKELEKKHQQLCEEKNAL-----------QEQLQAETELCAEAEEMRARLAARKQELEEILHELEs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 444 ELKEGLRQRDELIEEKQRMQQKIDTMTKEVFD-------LQETLLWKDKKIGALEKQ----KEYIACLRNERDMLREELA 512
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEeeaarqkLQLEKVTTEAKIKKLEEDilllEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 513 DLQETVKTGEKHGLVIIPDGTpngdvSHEPVagaitVVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLE 592
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLKN-----KHEAM-----ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 593 EERQKCSRNDgtvgdlaglqngsdlqfiEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVE 672
Cdd:pfam01576 233 ELRAQLAKKE------------------EELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQR 294
|
330
....*....|....*....
gi 530373301 673 DELKAEKRKLQRELRTALD 691
Cdd:pfam01576 295 RDLGEELEALKTELEDTLD 313
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
345-677 |
2.13e-03 |
|
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: 41.59 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 345 RDIYDLKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVsnaQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFyrENEEK 424
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL---RVKEKIGELEAEIASLERSIAEKERELEDA--EERLA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 425 SKELERQKhmcsvLQHKMEELKEGL----RQRDELIEEKQRMQQKIDTMTKEVFDLQETL-LWKDKkigaLEKQKEYIAC 499
Cdd:TIGR02169 326 KLEAEIDK-----LLAEIEELEREIeeerKRRDKLTEEYAELKEELEDLRAELEEVDKEFaETRDE----LKDYREKLEK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 500 LRNERDMLREELADLQETVKTGEKHGLVIipdgtpngdvshepvagaitvvsQEAAQVLESagegpldvRLRKLAGEKEE 579
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADL-----------------------NAAIAGIEA--------KINELEEEKED 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 580 LLSQIRKLKLQLEeerqkcsrndgtvgdlaglqngsdlQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVL 659
Cdd:TIGR02169 446 KALEIKKQEWKLE-------------------------QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
330
....*....|....*...
gi 530373301 660 RYKTAAENAEKVEDELKA 677
Cdd:TIGR02169 501 ASEERVRGGRAVEEVLKA 518
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
569-714 |
2.26e-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: 40.29 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 569 RLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVG------DLAGLQngSDLQFIEMQR-DANRQISEYKFKLSKAE 641
Cdd:COG1579 46 RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnkEYEALQ--KEIESLKRRIsDLEDEILELMERIEELE 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530373301 642 QDITTLEQSISRLEGQVLRYKTAAENAEKvedELKAEKRKLQRELRTALDKIEEmemtnsHLAKRLEKMKANR 714
Cdd:COG1579 124 EELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEAEREELAAKIPP------ELLALYERIRKRK 187
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
566-721 |
3.37e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 566 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCS-------RNDGTVGDLAGLQNGSDLQ-FIE-------MQRDANRQI 630
Cdd:COG3883 56 LQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralyRSGGSVSYLDVLLGSESFSdFLDrlsalskIADADADLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 631 SEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKM 710
Cdd:COG3883 136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
170
....*....|.
gi 530373301 711 KANRTALLAQQ 721
Cdd:COG3883 216 AAAAAAAAAAA 226
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
403-480 |
4.19e-03 |
|
Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.
Pssm-ID: 428400 [Multi-domain] Cd Length: 188 Bit Score: 38.79 E-value: 4.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530373301 403 LKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKeglRQRDELIEEKQRMQQKIDTMTKEVFDLQETL 480
Cdd:pfam05266 100 LKDRQTKLLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELE---RQLALAKEKKEAADKEIARLKSEAEKLEQEI 174
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
361-714 |
4.83e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 40.34 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 361 YMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQH 440
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 441 KMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETllWKDKKIGALEKQKEYIACLRNERDMLREELADLQETVKT 520
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE--ELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 521 GEKHglviipdgtpngdvshepvagaitvVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQ--KC 598
Cdd:pfam02463 326 AEKE-------------------------LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLakKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 599 SRNDGTVGDLAGL-QNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKA 677
Cdd:pfam02463 381 LESERLSSAAKLKeEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350
....*....|....*....|....*....|....*..
gi 530373301 678 EKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANR 714
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEE 497
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
362-447 |
4.85e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 39.71 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 362 MQGLKELKESLSEVEEKYKkamvsnaQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHK 441
Cdd:COG4026 127 IPEYNELREELLELKEKID-------EIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSR 199
|
....*.
gi 530373301 442 MEELKE 447
Cdd:COG4026 200 FEELLK 205
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
419-716 |
4.92e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 419 RENEEKSKELERQKhmcSVLQHKMEELKEglrQRDELIEEKQRMQQKIDTMTKEVFDLQEtllwkdkKIGALEKQK---- 494
Cdd:COG1340 4 DELSSSLEELEEKI---EELREEIEELKE---KRDELNEELKELAEKRDELNAQVKELRE-------EAQELREKRdeln 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 495 EYIACLRNERDMLREELADLQETVKTGEKHGLVIIPDGTPngdvshepvagaITVVSQEAAQVLESAGEGPLDVrlrkla 574
Cdd:COG1340 71 EKVKELKEERDELNEKLNELREELDELRKELAELNKAGGS------------IDKLRKEIERLEWRQQTEVLSP------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 575 gEKE-ELLSQIRKLKLQLEEERQKCSRNDgtvgDLAGLQNGSDLQFIEMqRDANRQISEYKFKLSKAEQDITTLEQSISR 653
Cdd:COG1340 133 -EEEkELVEKIKELEKELEKAKKALEKNE----KLKELRAELKELRKEA-EEIHKKIKELAEEAQELHEEMIELYKEADE 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530373301 654 LEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTA 716
Cdd:COG1340 207 LRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKA 269
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
343-684 |
5.54e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 343 ELRDIYDLKDQIQDVEGRYMQGLKELKES------LSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDV-----IEEQE 411
Cdd:TIGR00618 227 ELKHLREALQQTQQSHAYLTQKREAQEEQlkkqqlLKQLRARIEELRAQEAVLEETQERINRARKAAPLAahikaVTQIE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 412 EQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKID--TMTKEVFDLQETLLwkdKKIGA 489
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEvaTSIREISCQQHTLT---QHIHT 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 490 LEKQKEYIACLRNERDMLREELADLQETVKTgekhglviiPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEG----- 564
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQREQATIDT---------RTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCtaqce 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 565 ----PLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKcsrndgtvgdlaglqngsDLQFIEMQRDANRQISEYKFKLSKA 640
Cdd:TIGR00618 455 klekIHLQESAQSLKEREQQLQTKEQIHLQETRKKAV------------------VLARLLELQEEPCPLCGSCIHPNPA 516
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 530373301 641 EQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQR 684
Cdd:TIGR00618 517 RQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRAS 560
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
345-520 |
5.81e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.84 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 345 RDIYDLKDQIQDVEGRY---MQGLKELKESLSEVEEKYKKAMVSNAQLDNE--KNNLIY--QVDTLKDVIEEQEEQMAEF 417
Cdd:pfam06160 86 KALDEIEELLDDIEEDIkqiLEELDELLESEEKNREEVEELKDKYRELRKTllANRFSYgpAIDELEKQLAEIEEEFSQF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 418 YRENE-----EKSKELERQKHMCSVLQHKMEELKEGLRQ-RDELIEEKQRMQQKIDTMTKEVFDLQETLLwkDKKIGALE 491
Cdd:pfam06160 166 EELTEsgdylEAREVLEKLEEETDALEELMEDIPPLYEElKTELPDQLEELKEGYREMEEEGYALEHLNV--DKEIQQLE 243
|
170 180 190
....*....|....*....|....*....|.
gi 530373301 492 KQ-KEYIACLRN-ERDMLREELADLQETVKT 520
Cdd:pfam06160 244 EQlEENLALLENlELDEAEEALEEIEERIDQ 274
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
338-597 |
6.32e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 338 DTSLSELRD-----IYDLKDQIQDVEGR----YMQGLKELKESLSEVEEKYKKAmvsnaqldnEKNNLIYQVDTLKDVIE 408
Cdd:PRK05771 19 DEVLEALHElgvvhIEDLKEELSNERLRklrsLLTKLSEALDKLRSYLPKLNPL---------REEKKKVSVKSLEELIK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 409 EQEEQMAEFYRENEEKSKELErqkhmcsvlqhkmeelkeglrqrdELIEEKQRMQQKIDTMTK-EVFDLQETLLWKDKKI 487
Cdd:PRK05771 90 DVEEELEKIEKEIKELEEEIS------------------------ELENEIKELEQEIERLEPwGNFDLDLSLLLGFKYV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 488 ----GALEKQKEyiaclrnERDMLREELADLQETVKTGEKHGLVIIPDgtpngdvshepvAGAITVVSQEAAQV----LE 559
Cdd:PRK05771 146 svfvGTVPEDKL-------EELKLESDVENVEYISTDKGYVYVVVVVL------------KELSDEVEEELKKLgferLE 206
|
250 260 270
....*....|....*....|....*....|....*...
gi 530373301 560 SAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQK 597
Cdd:PRK05771 207 LEEEGTPSELIREIKEELEEIEKERESLLEELKELAKK 244
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
402-524 |
6.63e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 402 TLKDVIEEQEEqmaefyrenEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQrmqqkidtmtKEVFDLQETLL 481
Cdd:COG2433 377 SIEEALEELIE---------KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELE 437
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 530373301 482 WKDKKIGALE------KQKEY--------IACLRNERDMLREELADLQETVKTGEKH 524
Cdd:COG2433 438 EKDERIERLErelseaRSEERreirkdreISRLDREIERLERELEEERERIEELKRK 494
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
355-721 |
6.66e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 355 QDVEGRYMQGLKELKESLSEVEEKYKKAMvsnaQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHm 434
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEHNLSKIM----KLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQ- 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 435 csvlqhkmeelkeglRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEYIACLRNERDMLREELADL 514
Cdd:TIGR00606 312 ---------------RTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 515 QETvktgekhglviipDGTPNGDVSHEPVAGAITVV----SQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQ 590
Cdd:TIGR00606 377 LEL-------------DGFERGPFSERQIKNFHTLVierqEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 591 LEEER--QKCSRNDGTVGDLAGLQNGSDlqfiemqrdanrQISEYKFKLSKAEQDITTLEQSisrlegqvlrykTAAENA 668
Cdd:TIGR00606 444 LKKEIleKKQEELKFVIKELQQLEGSSD------------RILELDQELRKAERELSKAEKN------------SLTETL 499
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 530373301 669 EKVEDELKAEKRKLQRELRtALDkiEEMEMTNSHLAKRLEKMKANRTALLAQQ 721
Cdd:TIGR00606 500 KKEVKSLQNEKADLDRKLR-KLD--QEMEQLNHHTTTRTQMEMLTKDKMDKDE 549
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
365-525 |
7.06e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.03 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 365 LKELKESLSEVEEKYKKAMvsnAQLDNEKNNLIYQvdTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEE 444
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQA---AKLQGSDLDRTVQ--QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 445 LKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALE--------KQKEYIACLRNERDMLREELADLQE 516
Cdd:TIGR00606 869 LKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLEtflekdqqEKEELISSKETSNKKAQDKVNDIKE 948
|
....*....
gi 530373301 517 TVKtgEKHG 525
Cdd:TIGR00606 949 KVK--NIHG 955
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
422-519 |
7.93e-03 |
|
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.
Pssm-ID: 464008 [Multi-domain] Cd Length: 177 Bit Score: 37.97 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 422 EEKSKELERQKHMCSVLQHKMEELKEglrQRDELIEEKQRMQQKIDTMTKEVFDLQETLL-------WKDKKIGALEKQK 494
Cdd:pfam13870 59 EERNKELKRLKLKVTNTVHALTHLKE---KLHFLSAELSRLKKELRERQELLAKLRKELYrvklerdKLRKQNKKLRQQG 135
|
90 100 110
....*....|....*....|....*....|....*
gi 530373301 495 E----------YIAClRNERDMLREELADLQETVK 519
Cdd:pfam13870 136 GllhvpallhdYDKT-KAEVEEKRKSVKKLRRKVK 169
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
338-712 |
8.14e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 8.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 338 DTSLSELRDIYDLKD-QIQDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAE 416
Cdd:PRK02224 292 EEERDDLLAEAGLDDaDAEAVEAR----REELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 417 FYRENEEKSKELERQKHMCSVLQHKMEELKEGL-----------RQRDELIEEKQRMQQKIDTMTKEVFDLQ------ET 479
Cdd:PRK02224 368 LESELEEAREAVEDRREEIEELEEEIEELRERFgdapvdlgnaeDFLEELREERDELREREAELEATLRTARerveeaEA 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 480 LLWKDK------------KIGALEKQKEYIACLRNERDMLREELADLQETVKTGEKhgLVIIPDGTP----NGDVSHEPV 543
Cdd:PRK02224 448 LLEAGKcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAED--LVEAEDRIErleeRREDLEELI 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 544 AGAITVV---------SQEAAQVLESAGEGPLDvRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQN- 613
Cdd:PRK02224 526 AERRETIeekreraeeLRERAAELEAEAEEKRE-AAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADa 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 614 GSDLQFIEMQRDA-NRQISEYKFKLSKAEQDITTLEQSI--SRLEGQVLRYKTAAENAEKVE---DELKAEKRKLQRE-- 685
Cdd:PRK02224 605 EDEIERLREKREAlAELNDERRERLAEKRERKRELEAEFdeARIEEAREDKERAEEYLEQVEeklDELREERDDLQAEig 684
|
410 420
....*....|....*....|....*...
gi 530373301 686 -LRTALDKIEEMEMTNSHLAKRLEKMKA 712
Cdd:PRK02224 685 aVENELEELEELRERREALENRVEALEA 712
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
373-703 |
8.74e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.12 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 373 SEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKhmcSVLQHKMEELKEGLRQR 452
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN---EQLQAAQAELAQAQEEL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 453 DELIEEKQRMQQKIDTMTKEVFDLQETllwKDKKIGALEKQKEYIACLRNERDMLREELADLQETVKTGEKHGLVIIPDG 532
Cdd:COG4372 104 ESLQEEAEELQEELEELQKERQDLEQQ---RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 533 TPNGDVSHEPVAGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQ 612
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530373301 613 NGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDK 692
Cdd:COG4372 261 EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
330
....*....|.
gi 530373301 693 IEEMEMTNSHL 703
Cdd:COG4372 341 DLLQLLLVGLL 351
|
|
| |
