|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
277-631 |
1.23e-102 |
|
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: 316.25 E-value: 1.23e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 277 LDEKSDKQYAENYT---------RPSSRNSASATTPLSGNSSRRGSGDTSSLIDPDTSLSELRDiydlkdqiqdvegrym 347
Cdd:pfam09738 30 VEENADRVFDMSSSsgadtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKH---------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 348 qglkelkeSLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKM 427
Cdd:pfam09738 94 --------ELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 428 EELKEGLRQRDELIeekqrmqqkidtmtkevfdlqetllwkdkkigalekqkeyiaclrnerdmlreeladlqetvktgE 507
Cdd:pfam09738 166 AELKEQLKQRDELI-----------------------------------------------------------------E 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 508 KHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQ-KCSRN 586
Cdd:pfam09738 181 KHGLVIVPDENTNGEEENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKSkRNSTR 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 578806708 587 DGTVGDLAGLQNGSDLqfIEMQRDANRQISEYKFKLSKAEQDITT 631
Cdd:pfam09738 261 SSQSPDGFGLENGSHV--IEVQREANKQISDYKFKLQKAEQEITT 303
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
304-682 |
1.78e-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: 67.79 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 304 LSGNSSRRGSGDTSSLIDPDTSLSELRDIYDLKDQ---IQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNN 380
Cdd:TIGR02169 655 MTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRElssLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 381 LIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQrdELIEEKQRMQQKIDtmtKEVFD 460
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLE---EEVSR 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 461 LQETLLWKDKKIGALEKQKEYiacLRNERDMLREELADLQETVKTGEKhglviipdgtpNGDVSHEPVAGAITVVSQEAA 540
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEY---LEKEIQELQEQRIDLKEQIKSIEK-----------EIENLNGKKEELEEELEELEA 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 541 QVLEsagegpLDVRLRKLAGEKEELLSQIRKLKL---QLEEERQKCSRNDGTVGDLAGLQNGsDLQFIEMQRDANRQISE 617
Cdd:TIGR02169 876 ALRD------LESRLGDLKKERDELEAQLRELERkieELEAQIEKKRKRLSELKAKLEALEE-ELSEIEDPKGEDEEIPE 948
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578806708 618 YKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEME 682
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
350-681 |
6.75e-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: 62.77 E-value: 6.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 350 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEE 429
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 430 LKEglrQRDELIEEKQRMQQKIDTMTKEVFDLQETLlwkDKKIGALEKQKEYIACLRNERDMLREELADLQETVKTGEKh 509
Cdd:TIGR02168 759 LEA---EIEELEERLEEAEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLESLER- 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 510 glviipdgtpngdvSHEPVAGAITVVSQEAAQVLEsagegpldvRLRKLAGEKEELLSQIRKLKLQLEE-ERQKCSRNDG 588
Cdd:TIGR02168 832 --------------RIAATERRLEDLEEQIEELSE---------DIESLAAEIEELEELIEELESELEAlLNERASLEEA 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 589 TVGDLAGLQN-GSDLQFIEMQR-DANRQISEYKFKLSKAEQDITTLEQSISRLEGQVL-RYKTAAENAEKVEDELKAEKR 665
Cdd:TIGR02168 889 LALLRSELEElSEELRELESKRsELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEE 968
|
330
....*....|....*.
gi 578806708 666 KLQRELRTALDKIEEM 681
Cdd:TIGR02168 969 EARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
311-681 |
8.16e-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: 8.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 311 RGSGDTSSLIdpdtsLSELRDIYDLKDQIQDVEGRYMQGLKELKESLSEVEEkYKKAMVSNAQLDNEKNNLIYQVDTLKD 390
Cdd:TIGR02168 663 GGSAKTNSSI-----LERRREIEELEEKIEELEEKIAELEKALAELRKELEE-LEEELEQLRKELEELSRQISALRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 391 VIEEQEEQMAEFYRENEEKSKELERQKhmcSVLQHKMEELKEGLrqrDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDK 470
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEI---EELEERLEEAEEEL---AEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 471 KIGALE----KQKEYIACLRNERDMLREELADLQETVKTGEKHGLVI---IPDGTPNGDVSHEPVAGAITVV-SQEAAQV 542
Cdd:TIGR02168 811 ELTLLNeeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEALLNERaSLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 543 LESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLagLQNGSDLQFIEMQrDANRQISEYKFKL 622
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL--QERLSEEYSLTLE-EAEALENKIEDDE 967
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 623 SKAEQDITTLEQSISRLeGQV-LRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEM 681
Cdd:TIGR02168 968 EEARRRLKRLENKIKEL-GPVnLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
350-682 |
3.17e-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: 57.37 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 350 LKELKESL------SEVEEKYKkamvsnaQLDNEKNNLiyQVDTLKDVIEEQEEQMAEF---YRENEEKSKELERQKHMc 420
Cdd:TIGR02168 195 LNELERQLkslerqAEKAERYK-------ELKAELREL--ELALLVLRLEELREELEELqeeLKEAEEELEELTAELQE- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 421 svLQHKMEELKEGLRQRDELIEEKQR----MQQKIDTMTKEVFDLQETLLWKDKKIGALEkqkEYIACLRNERDMLREEL 496
Cdd:TIGR02168 265 --LEEKLEELRLEVSELEEEIEELQKelyaLANEISRLEQQKQILRERLANLERQLEELE---AQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 497 ADLQETVKTGEKhglviipdgtpngdvSHEPVAGAITvVSQEAAQVLESAGEGpLDVRLRKLAGEKEELLSQIRKLKLQL 576
Cdd:TIGR02168 340 AELEEKLEELKE---------------ELESLEAELE-ELEAELEELESRLEE-LEEQLETLRSKVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 577 EEERQKCSRNDGTVGdlaglqngsdlQFIEMQRDANRQISEYKFKLSKAEqdITTLEQSISRLEGQVLRYKTAAENAEKV 656
Cdd:TIGR02168 403 ERLEARLERLEDRRE-----------RLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEALEELREE 469
|
330 340
....*....|....*....|....*.
gi 578806708 657 EDELKAEKRKLQRELRTALDKIEEME 682
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLE 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
404-653 |
8.76e-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: 8.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 404 RENEEKSKELERQkhmcsvLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQkeyIA 483
Cdd:COG4942 23 AEAEAELEQLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE---IA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 484 CLRNERDMLREELAD-LQETVKTGEKHGL-VIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEgpldvRLRKLAGE 561
Cdd:COG4942 94 ELRAELEAQKEELAElLRALYRLGRQPPLaLLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----ELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 562 KEELLSQIRKLKLQLEEERQKcsrndgtvgdLAGLQNGSDlqfiEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEG 641
Cdd:COG4942 169 LEAERAELEALLAELEEERAA----------LEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
250
....*....|..
gi 578806708 642 QVLRYKTAAENA 653
Cdd:COG4942 235 EAAAAAERTPAA 246
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
333-508 |
4.63e-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: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 333 YDLKDQIQDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKE 412
Cdd:TIGR02168 291 YALANEISRLEQQ----KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 413 LErqkhmcsVLQHKMEELKEGL-RQRDELIEEKQRMQQ---KIDTMTKEVFDLQETL---------LWKDKKIGALEKQK 479
Cdd:TIGR02168 367 LE-------ELESRLEELEEQLeTLRSKVAQLELQIASlnnEIERLEARLERLEDRRerlqqeieeLLKKLEEAELKELQ 439
|
170 180
....*....|....*....|....*....
gi 578806708 480 EYIACLRNERDMLREELADLQETVKTGEK 508
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELRE 468
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
336-599 |
6.51e-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: 49.67 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 336 KDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKN-------NLIYQVDTLKDVIEEQEEQMAEFYRENEE 408
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 409 KSKELERQKhmcSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQ----KEYIAC 484
Cdd:TIGR02168 321 LEAQLEELE---SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqlELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 485 LRNERDMLREELADLQETVktgEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEgpLDVRLRKLAGEKEE 564
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRR---ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELER--LEEALEELREELEE 472
|
250 260 270
....*....|....*....|....*....|....*
gi 578806708 565 LLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNG 599
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
384-697 |
6.61e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 384 QVDTLKDVIEEQEEQMAEFYRENEEKSKELErqkhmcsvLQHKMEELK--EGLRQRDELIEEKQRMQQKIDTMTKEVFDL 461
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLERLRREREKAERYQA--------LLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 462 QETLLWKDKKIGALEKQKEYIAclRNERDMLREELADLQETVktGEKHGLViipdgtpngdvshEPVAGAITVVSQEAAQ 541
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKI--GELEAEI-------------ASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 542 vlesagegpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNG--SDLQFIEMQRDANRQ-ISEY 618
Cdd:TIGR02169 320 ---------AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDlrAELEEVDKEFAETRDeLKDY 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806708 619 KFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 697
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
388-706 |
6.69e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 6.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 388 LKDVIEEQEEQM---------AEFYRENEEKSKELERQkhmcsVLQHKMEELKEGLRQRDELIEEKQRMQQKIDtmtkev 458
Cdd:COG1196 191 LEDILGELERQLeplerqaekAERYRELKEELKELEAE-----LLLLKLRELEAELEELEAELEELEAELEELE------ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 459 fdlqetllwkdKKIGALEKQKEYiacLRNERDMLREELADLQEtvktgekhglviipdgtpngdvshepvagAITVVSQE 538
Cdd:COG1196 260 -----------AELAELEAELEE---LRLELEELELELEEAQA-----------------------------EEYELLAE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 539 AAQvlESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQkcsrndgtvgdlaglqngsdlqfiemqrdanrQISEY 618
Cdd:COG1196 297 LAR--LEQDIARLEERRRELEERLEELEEELAELEEELEELEE--------------------------------ELEEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 619 KFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKAN 698
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
....*...
gi 578806708 699 RTALLAQQ 706
Cdd:COG1196 423 LEELEEAL 430
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
334-697 |
9.27e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 9.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 334 DLKDQIQDVE--------GRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEF 402
Cdd:PRK02224 191 QLKAQIEEKEekdlherlNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 403 YRENEEKSKELERQKHMCSVLqhkmEELKEGLRQRDELIE-EKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEy 481
Cdd:PRK02224 271 EREREELAEEVRDLRERLEEL----EEERDDLLAEAGLDDaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAE- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 482 iaCLRNERDMLREELADLQETVKTGEKhglviipdGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGPldVRLRKLAGE 561
Cdd:PRK02224 346 --SLREDADDLEERAEELREEAAELES--------ELEEAREAVEDRREEIEELEEEIEELRERFGDAP--VDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 562 KEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDL----QFIEMQRDANRqISEYKFKLSKAEQDITTLEQSIS 637
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgQPVEGSPHVET-IEEDRERVEELEAELEDLEEEVE 492
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806708 638 RLEGQVLRYKTAAENAEKVEDelKAEKRKLQRELR-TALDKIEEMEMTNSHLAKRLEKMKA 697
Cdd:PRK02224 493 EVEERLERAEDLVEAEDRIER--LEERREDLEELIaERRETIEEKRERAEELRERAAELEA 551
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
334-697 |
9.94e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 334 DLKDQIQDVEGRYMQGLKELKESLSEVE---------EKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYR 404
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPelreeleklEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 405 ENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQEtllwkdkKIGALEKQKEYIAC 484
Cdd:PRK03918 270 ELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE-------RIKELEEKEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 485 LRNERDMLREELADLQETVKTGEKhglviipdgtpngdvshepvAGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEE 564
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEE--------------------AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 565 LLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQI-SEYKFKLSKAEQDITTLEQSISRL---- 639
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLrkel 482
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806708 640 ---------EGQVLRYKTAAENAEKVEDELKA----EKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 697
Cdd:PRK03918 483 relekvlkkESELIKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
330-705 |
1.39e-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: 48.51 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 330 RDIYDLKDQIQDVEgrymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQM-------AEF 402
Cdd:TIGR02168 316 RQLEELEAQLEELE----SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLetlrskvAQL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 403 YRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQR--MQQKIDTMTKEVFDLQETLlwkDKKIGALEKQKE 480
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEEL---ERLEEALEELRE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 481 YIACLRNERDMLREELA-----------------DLQETVKTGEKHGLVIIPDGTPNGD-VSHEP------------VAG 530
Cdd:TIGR02168 469 ELEEAEQALDAAERELAqlqarldslerlqenleGFSEGVKALLKNQSGLSGILGVLSElISVDEgyeaaieaalggRLQ 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 531 AITVVSQEAA----QVLESAGEG-----PLD-VRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAG----- 595
Cdd:TIGR02168 549 AVVVENLNAAkkaiAFLKQNELGrvtflPLDsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGgvlvv 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 596 --LQNGSDLQ--------FIEMQ--------------RDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAE 651
Cdd:TIGR02168 629 ddLDNALELAkklrpgyrIVTLDgdlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELE 708
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 578806708 652 NAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 705
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
331-550 |
1.39e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 331 DIYDLKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEFYRENE 407
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEalqAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 408 EKSKE----------------LERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETllwKDKK 471
Cdd:COG3883 97 RSGGSvsyldvllgsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA---KAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806708 472 IGALEKQKEYIACLRNERDMLREELADLQETVKTGEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGP 550
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
551-705 |
1.49e-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: 46.84 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 551 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAglqngSDLQFIEMQ-RDANRQISEYKFKLSKA---- 625
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-----KEIKRLELEiEEVEARIKKYEEQLGNVrnnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 626 -----EQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEmtnSHLAKRLEKMKANRT 700
Cdd:COG1579 90 eyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAELEELEAERE 166
|
....*
gi 578806708 701 ALLAQ 705
Cdd:COG1579 167 ELAAK 171
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
328-699 |
2.50e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 328 ELRDIYDLKDQIQDVEGRymqgLKELKESLSEVEEK---YKKAMVSNAQLDNEKNNL-IYQVDTLKDVIEEQEEQMAEFY 403
Cdd:PRK03918 329 RIKELEEKEERLEELKKK----LKELEKRLEELEERhelYEEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 404 RENEEKSKELERQKHMCSVLQHKMEELKEGLRQ----RDELIEEKQrmQQKIDTMTKEVFDLQETLLWKDKKIGALEKQK 479
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 480 EYI-ACLRNERDMLR-EELAD-LQETVKTGEKHGLVIIPDGTPNGDVSHEPVAGaitvVSQEAAQVLESAGEG-PLDVRL 555
Cdd:PRK03918 483 RELeKVLKKESELIKlKELAEqLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK----LKGEIKSLKKELEKLeELKKKL 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 556 RKLAGEKEELLSQIRKLKLQLEEERQKCSRN-DGTVGDLAGLQNgsdlQFIEMqRDANRQISEYKFKLSKAEQDITTLEQ 634
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGFESVEElEERLKELEPFYN----EYLEL-KDAEKELEREEKELKKLEEELDKAFE 633
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 635 SISRLEGQVLRYKTAAENAEKVEDE-----LKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANR 699
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
400-683 |
2.56e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 400 AEFYRENEEKSKELERQKHMCSVLQHKMEELKEglrQRDELIEEKQRmQQKIDTMTKEVFDLQETLLWKDKKigALEKQK 479
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREK-AERYQALLKEKREYEGYELLKEKE--ALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 480 EYIaclRNERDMLREELADLQETVKTGEKHglviipdgtpngdvshepVAGAITVVSQEAAQVLESAGEGPLDVR--LRK 557
Cdd:TIGR02169 240 EAI---ERQLASLEEELEKLTEEISELEKR------------------LEEIEQLLEELNKKIKDLGEEEQLRVKekIGE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 558 LAGEKEELLSQIRKLKLQLE----EERQKCSRNDGTVGDLAGLQngSDLQFIEMQRDA-NRQISEYKFKLSKAEQDITTL 632
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEdaeeRLAKLEAEIDKLLAEIEELE--REIEEERKRRDKlTEEYAELKEELEDLRAELEEV 376
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 578806708 633 EQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEM 683
Cdd:TIGR02169 377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
326-702 |
2.63e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 326 LSELRDIYDLKDQIQDVEGRYmqglKELKESLSEVEEKYKKAMVSNAQLDNEKNNLiyqvdtlkdvieEQEEQMAEFYRE 405
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKL------------EKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 406 NEEKSKELERqkhmcsvLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKigALEKQKEYIACL 485
Cdd:COG4717 134 LEALEAELAE-------LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE--ELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 486 RNERDMLREELADLQETVKTGEKH----------------------------GLVIIPDGTPNGDVSHEPVAGAITVV-- 535
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEEleqleneleaaaleerlkearlllliaaALLALLGLGGSLLSLILTIAGVLFLVlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 536 ---------SQEAAQVLESAGEGPLDVRLRKLAGEK-------------------EELLSQIRKLKL------QLEEERQ 581
Cdd:COG4717 285 llallflllAREKASLGKEAEELQALPALEELEEEEleellaalglppdlspeelLELLDRIEELQEllreaeELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 582 KCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQIsEYKFKLSKAEQDITTLEQSI---------SRLEGQVLRYKTAAEN 652
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELeellealdeEELEEELEELEEELEE 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 578806708 653 AEKVEDELKAEKRKLQRELRT---------ALDKIEEMEMTNSHLAKRLEKMKANRTAL 702
Cdd:COG4717 444 LEEELEELREELAELEAELEQleedgelaeLLQELEELKAELRELAEEWAALKLALELL 502
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
331-702 |
2.81e-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: 47.32 E-value: 2.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 331 DIYDLKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEK---NNLIYQVDTLKDVIEEQEEQMAEFYRENE 407
Cdd:TIGR04523 69 KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKeqkNKLEVELNKLEKQKKENKKNIDKFLTEIK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 408 EKSKELERQKHMCSVLQHKMEELKEglrQRDELIEEKQRMQQKIDTMTKEVFDLQETLL---WKDKKIGALEKQ----KE 480
Cdd:TIGR04523 149 KKEKELEKLNNKYNDLKKQKEELEN---ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSnlkKKIQKNKSLESQiselKK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 481 YIACLRNERDMLREELADLQETVKTGEKHGLVIIPDGTPNGDVSHEP---VAGAITVVSQEAAQVLEsagegpLDVRLRK 557
Cdd:TIGR04523 226 QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKqkeLEQNNKKIKELEKQLNQ------LKSEISD 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 558 LAGEKE-----ELLSQIRKLKLQLEEERQKCSRNDGTVGDLaglqnGSDLQFIEMQRD--------ANRQISEYKFKLSK 624
Cdd:TIGR04523 300 LNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQL-----NEQISQLKKELTnsesenseKQRELEEKQNEIEK 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578806708 625 AEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTAL 702
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
484-706 |
3.52e-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: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 484 CLRNERDMLREELADLQETVKTGEKhglviipdgtpngdvshepvagAITVVSQEAAQVLEsagegpldvRLRKLAGEKE 563
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEK----------------------ALAELRKELEELEE---------ELEQLRKELE 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 564 ELLSQIRKLKLQLEEERQKCSRndgtVGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQV 643
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806708 644 LRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 706
Cdd:TIGR02168 799 KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
334-508 |
4.14e-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: 4.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 334 DLKDQIQDVEgrymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 413
Cdd:pfam07888 77 ELESRVAELK----EELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 414 ERQKhmcsvlqhkmEELKEGLRQRDELIEEKQRMQQKIDTMTKEV----FDLQETLLWKDKKIGALEKQKEYIACLRN-- 487
Cdd:pfam07888 153 ERMK----------ERAKKAGAQRKEEEAERKQLQAKLQQTEEELrslsKEFQELRNSLAQRDTQVLQLQDTITTLTQkl 222
|
170 180
....*....|....*....|....*....
gi 578806708 488 --------ERDMLREELADLQETVKTGEK 508
Cdd:pfam07888 223 ttahrkeaENEALLEELRSLQERLNASER 251
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
335-706 |
4.70e-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: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 335 LKDQIQDVEGRYMQGL-KELKESLSEVEEKYKkamvsnaQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 413
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWnKELKSELKNQEKKLE-------EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 414 ERqkhmcsvlqhKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEYiacLRNERDMLR 493
Cdd:TIGR04523 366 EE----------KQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL---LEKEIERLK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 494 EELADLQETVKTGEKhglviipdgtpngdvshepvagaitvvsQEAAqvlesagegpLDVRLRKLAGEKEELLSQIRKLK 573
Cdd:TIGR04523 433 ETIIKNNSEIKDLTN----------------------------QDSV----------KELIIKNLDNTRESLETQLKVLS 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 574 LQLEEERQKCSRNdgtvgdlaglqngsdlqfiemqrdanrqiseyKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENA 653
Cdd:TIGR04523 475 RSINKIKQNLEQK--------------------------------QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSL 522
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578806708 654 EKVEDELKAEKRKLQRELRTALDKIEEMEMTN---------SHLAKRLEKMKANRTALLAQQ 706
Cdd:TIGR04523 523 KEKIEKLESEKKEKESKISDLEDELNKDDFELkkenlekeiDEKNKEIEELKQTQKSLKKKQ 584
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
551-697 |
7.12e-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: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 551 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCsrnDGTVGDLAGlQNGSDLQFIEMQ-RDANRQISEYKFKLSKAEQDI 629
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREEL---DELEAQIRG-NGGDRLEQLEREiERLERELEERERRRARLEALL 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806708 630 TTLEQSI-----------SRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 697
Cdd:COG4913 369 AALGLPLpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
348-689 |
7.98e-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: 45.97 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 348 QGLKELKESLSEVEEKykkamvsnaqldneKNNLIYQVDTLKDVIEEQEEQMAE----FYRENEEKSK---ELERQKHM- 419
Cdd:pfam10174 324 QHIEVLKESLTAKEQR--------------AAILQTEVDALRLRLEEKESFLNKktkqLQDLTEEKSTlagEIRDLKDMl 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 420 ------CSVLQHKMEELKEGLRQRDELIEEKQR----MQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEYI-ACLRNE 488
Cdd:pfam10174 390 dvkerkINVLQKKIENLQEQLRDKDKQLAGLKErvksLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREdRERLEE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 489 RDMLREELADLQETVKTGEKHGL----VIIPDGTPNGDVSHEPVAGAITVVSQEAAqvLESAGEGP--LDVRLRKL---- 558
Cdd:pfam10174 470 LESLKKENKDLKEKVSALQPELTekesSLIDLKEHASSLASSGLKKDSKLKSLEIA--VEQKKEECskLENQLKKAhnae 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 559 --AGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGL-------QNGSDLQFIEMQRDANRQISEykfkLSKAEQDI 629
Cdd:pfam10174 548 eaVRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGIlreveneKNDKDKKIAELESLTLRQMKE----QNKKVANI 623
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578806708 630 TTLEQSISRLEGQVLryktaaENAEKVEDELKAEKRKLQ-RELRTALDKI-EEMEMTNSHLA 689
Cdd:pfam10174 624 KHGQQEMKKKGAQLL------EEARRREDNLADNSQQLQlEELMGALEKTrQELDATKARLS 679
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
334-682 |
7.99e-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: 46.17 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 334 DLKDQIQDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 413
Cdd:TIGR04523 311 ELKSELKNQEKK----LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 414 ERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDtmtKEVFDLQETLLWKDKKIGALEKQ----KEYIACLRNER 489
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE---KEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTR 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 490 DMLREELADLQETVKTgEKHGLviipdgtpngdvshEPVAGAITVVSQEAAQVLESAGEgpLDVRLRKLAGEKEELLSQI 569
Cdd:TIGR04523 464 ESLETQLKVLSRSINK-IKQNL--------------EQKQKELKSKEKELKKLNEEKKE--LEEKVKDLTKKISSLKEKI 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 570 RKLKLQLEEERQKCSRNDgtvGDLAGLQNGSDLQFIEMQRDA-NRQISEYKF-------KLSKAEQDITTLEQSISRLEG 641
Cdd:TIGR04523 527 EKLESEKKEKESKISDLE---DELNKDDFELKKENLEKEIDEkNKEIEELKQtqkslkkKQEEKQELIDQKEKEKKDLIK 603
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 578806708 642 QVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEME 682
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
392-702 |
8.09e-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: 46.21 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 392 IEEQEEQMAEFYRENEEKSKELER------QKHMCSVLQHKMEELK--EGLRQRDELIEEKQRMQQKIDTMTKEVFDLQE 463
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERlrrereKAERYQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKLTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 464 TLLWKDKKIGALEKQKEYIAclRNERDMLREELADLQETVK--TGEKHGLV-IIPDGTPNGDVSHEPVAGAITVVSQEAA 540
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKIGelEAEIASLErSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 541 QVLESAGE-GPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKcsrNDGTVGDLAGLQNGSDlQFIEMQRDANRQISEYK 619
Cdd:TIGR02169 337 EIEELEREiEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE---FAETRDELKDYREKLE-KLKREINELKRELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 620 FKLSKAEQDITTLEQSISRLEGQVLRYKTAAENA----EKVEDELK---AEKRKLQRELRTALDKIEEMEMTNSHLAKRL 692
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKaleiKKQEWKLEqlaADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
330
....*....|
gi 578806708 693 EKMKANRTAL 702
Cdd:TIGR02169 493 AEAEAQARAS 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
539-706 |
8.82e-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: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 539 AAQVLESAGEG--PLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNgsdlQFIEMQRDANRQIS 616
Cdd:TIGR02168 230 LVLRLEELREEleELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY----ALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 617 EYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMK 696
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170
....*....|
gi 578806708 697 ANRTALLAQQ 706
Cdd:TIGR02168 386 SKVAQLELQI 395
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
331-680 |
1.20e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 331 DIYDLKDQIQDVEGRymqgLKELKESLSEVEE--KYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEE 408
Cdd:PRK03918 260 KIRELEERIEELKKE----IEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 409 KSKELERQKHMCSVLQHKMEELKEGLRQRDE---LIEEKQRMQQKIDTMTKEVFdlqetllwkDKKIGALEKQKEYIacl 485
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELYEEakaKKEELERLKKRLTGLTPEKL---------EKELEELEKAKEEI--- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 486 RNERDMLREELADLQETVKTGEKhglVIIPDGTPNGDVshePVAGAiTVVSQEAAQVLESAGEGPLDVR--LRKLAGEKE 563
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKK---AIEELKKAKGKC---PVCGR-ELTEEHRKELLEEYTAELKRIEkeLKEIEEKER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 564 ELLSQIRKLKLQLEEERqKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQV 643
Cdd:PRK03918 477 KLRKELRELEKVLKKES-ELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELK 555
|
330 340 350
....*....|....*....|....*....|....*..
gi 578806708 644 LRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEE 680
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELEELGFESVEELEE 592
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
357-695 |
1.55e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 357 LSEVEEKYKKAMVSNAQLDNEKNNL---IYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEG 433
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 434 LRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQ-----------KEYIAcLRNERDMLREELADLQET 502
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkelkekaEEYIK-LSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 503 vktgekhglviipdgtpngdvshepvagaITVVSQEAAQVLESAGEGPLDV-RLRKLAGEKEELLSQIRKLK---LQLEE 578
Cdd:PRK03918 316 -----------------------------LSRLEEEINGIEERIKELEEKEeRLEELKKKLKELEKRLEELEerhELYEE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 579 ERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQISEykfKLSKAEQDITTLEQSISRLEGQVLRYKTAAE-----NA 653
Cdd:PRK03918 367 AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEE---EISKITARIGELKKEIKELKKAIEELKKAKGkcpvcGR 443
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 578806708 654 EKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKM 695
Cdd:PRK03918 444 ELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
350-676 |
1.64e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 350 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQM----AEFYRENEEKSKELERQKHMCSVLQH 425
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 426 KMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLlwKDKKIGALEKQKEYIACLRNERDMLREELADLQEtvkt 505
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL--AEAEEALLEAEAELAEAEEELEELAEELLEALRA---- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 506 gekhglviipdgtpngdvshepvagaitvVSQEAAQVLEsagegpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSR 585
Cdd:COG1196 395 -----------------------------AAELAAQLEE------LEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 586 NDGTVGDLAGLQNGSDLQfiemQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAE-KVEDELKAEK 664
Cdd:COG1196 440 EEEALEEAAEEEAELEEE----EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALL 515
|
330
....*....|..
gi 578806708 665 RKLQRELRTALD 676
Cdd:COG1196 516 LAGLRGLAGAVA 527
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
475-702 |
1.64e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.05 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 475 LEKQKEYIACLRNERDMLREELADLQETVKTGEKHGLviipdgtpngDVSHEPVAGAITVVSQEAAQVLESAGEGPLDVR 554
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELE----------ELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 555 LRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQ----------ISEYKFKLSK 624
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeaanlrerLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 625 AEQDITTLEQSISRLEGQVLRY----KTAAENAEKVEDELKA---EKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 697
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLaaeiEELEELIEELESELEAllnERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
....*
gi 578806708 698 NRTAL 702
Cdd:TIGR02168 916 ELEEL 920
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
436-705 |
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 578806708 436 QRDELIEEKQRMQQKIDTMTKEVFDLQETllwKDKKIGALEKQKEYIACLRNERDMLREELADLQEtvktgekhglviip 515
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKE---EKALLKQLAALERRIAALARRIRALEQELAALEA-------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 516 dgtpngdvshepvagaitvvsqeaaqvlesagegpldvRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNdGTVGDLAG 595
Cdd:COG4942 84 --------------------------------------ELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLAL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 596 LQNGSDLQFIEMQRDANRQISEYKfklskaEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTAL 675
Cdd:COG4942 125 LLSPEDFLDAVRRLQYLKYLAPAR------REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQ 198
|
250 260 270
....*....|....*....|....*....|
gi 578806708 676 DKIEEMEMTNSHLAKRLEKMKANRTALLAQ 705
Cdd:COG4942 199 KLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
338-693 |
2.89e-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: 44.40 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 338 QIQDVEGRYMQGLKELKESLsEVEEKYKKAMVSNAQ-LDNEKNNLIYQVDTLkdvieEQEEQmaefyrENEEKSKELERQ 416
Cdd:pfam01576 346 QLQEMRQKHTQALEELTEQL-EQAKRNKANLEKAKQaLESENAELQAELRTL-----QQAKQ------DSEHKRKKLEGQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 417 khmcsvLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKE---------------- 480
Cdd:pfam01576 414 ------LQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQdtqellqeetrqklnl 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 481 --YIACLRNERDMLREELADLQETVKTGEKHGLviipdgtpngdvSHEPVAGAITVVSQEAAQVLESAGEGpldvrlrkl 558
Cdd:pfam01576 488 stRLRQLEDERNSLQEQLEEEEEAKRNVERQLS------------TLQAQLSDMKKKLEEDAGTLEALEEG--------- 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 559 ageKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGlqngsDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISr 638
Cdd:pfam01576 547 ---KKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ-----ELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAIS- 617
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 578806708 639 legqvLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLE 693
Cdd:pfam01576 618 -----ARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEME 667
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
350-699 |
3.13e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 350 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVI------------EEQEEQMAEFYRENEEKSKELERQK 417
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteEHRKELLEEYTAELKRIEKELKEIE 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 418 HMCSVLQHKMEELKEGLRQRDELIEEKQRMQQ--------------KIDTMTKEVFDLQETLLWKDKKIGALEKQKEYIA 483
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESELIKLKELAEQlkeleeklkkynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 484 CLRNERDMLREELADLQETVKTGEKHGLVIipdgtpnGDVSHEPVAGAItvvsqeaaQVLESAGEGPLdvRLRKLAGEKE 563
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEEL-------GFESVEELEERL--------KELEPFYNEYL--ELKDAEKELE 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 564 ELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNgsdlqfiemqrDANRQISEYKFKlsKAEQDITTLEQSISRLEGQV 643
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELE-----------ELEKKYSEEEYE--ELREEYLELSRELAGLRAEL 682
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 578806708 644 lryktaaENAEKVEDELKAEKRKLQRELRTALDKIEEMEMtnshLAKRLEKMKANR 699
Cdd:PRK03918 683 -------EELEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
334-505 |
3.19e-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: 44.24 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 334 DLKDQIQDVEGRY---MQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKS 410
Cdd:TIGR04523 465 SLETQLKVLSRSInkiKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 411 KELERQK------HMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQ-----K 479
Cdd:TIGR04523 545 DELNKDDfelkkeNLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKElekakK 624
|
170 180 190
....*....|....*....|....*....|..
gi 578806708 480 EY------IACLRNERDMLREELADLQETVKT 505
Cdd:TIGR04523 625 ENeklssiIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
326-458 |
3.51e-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: 42.60 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 326 LSELRDIYD-LKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQ-----VDTLKDVIEEQEEQM 399
Cdd:COG1579 33 LAELEDELAaLEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEalqkeIESLKRRISDLEDEI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 400 AEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQR-DELIEEKQRMQQKIDTMTKEV 458
Cdd:COG1579 113 LELMERIEELEEELAELEAELAELEAELEEKKAELDEElAELEAELEELEAEREELAAKI 172
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
401-696 |
4.87e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 401 EFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETllwkDKKIGALEKQKE 480
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL----KEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 481 YiacLRNERDMLREELADLQETVKTGEKHglviipdgtpngdvshepvagaITVVSQEAAQVLESAGEGPLDVRLRKLAG 560
Cdd:PRK03918 249 S---LEGSKRKLEEKIRELEERIEELKKE----------------------IEELEEKVKELKELKEKAEEYIKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 561 EKEELLSQIRKLKLQLEEERQKCSRNdgtvgdlaglqngsdlqfIEMQRDANRQISEYKFKLSKAEQDITTLE------Q 634
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEER------------------IKELEEKEERLEELKKKLKELEKRLEELEerhelyE 365
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578806708 635 SISRLEGQVLRYKT--AAENAEKVEDELK-AEKRK--LQRELRTALDKIEEMEMTNSHLAKRLEKMK 696
Cdd:PRK03918 366 EAKAKKEELERLKKrlTGLTPEKLEKELEeLEKAKeeIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
350-702 |
6.49e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.18 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 350 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQH---K 426
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvqtE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 427 MEELKEGLRQRDELIEekqRMQQKIDTMTKEVFDLQETllwkdkkIGALEKQKEYIACLRNERDMLREELADLQET--VK 504
Cdd:pfam15921 550 CEALKLQMAEKDKVIE---ILRQQIENMTQLVGQHGRT-------AGAMQVEKAQLEKEINDRRLELQEFKILKDKkdAK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 505 TGEKHGLViipdgtpnGDVSHEPV----AG-----AITVVSQEAAQVLESAGEG---------PLDVRLRKLAGEKEELL 566
Cdd:pfam15921 620 IRELEARV--------SDLELEKVklvnAGserlrAVKDIKQERDQLLNEVKTSrnelnslseDYEVLKRNFRNKSEEME 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 567 SQIRKLKLQLEEERQKCSRNDGTVGDLaglqNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISrlegqvlry 646
Cdd:pfam15921 692 TTTNKLKMQLKSAQSELEQTRNTLKSM----EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMT--------- 758
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 647 ktaaeNAEKVEDELKAEKRKLQRELRT-ALDKIE---EMEMTNSHLAKRLEKMKANRTAL 702
Cdd:pfam15921 759 -----NANKEKHFLKEEKNKLSQELSTvATEKNKmagELEVLRSQERRLKEKVANMEVAL 813
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
330-508 |
7.98e-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: 42.75 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 330 RDIYDLKDQIQDVEGRYMQGLKELKESLSEVEE---KYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYREN 406
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEElerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 407 EEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEkqrMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEYIAclr 486
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELAD---LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA--- 461
|
170 180
....*....|....*....|..
gi 578806708 487 NERDMLREELADLQETVKTGEK 508
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEK 483
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
382-576 |
9.01e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 382 IYQVDTLK--DVI---EEQEEQMAEFYRENEEKSKELERQKhmcSVLQHKMEELKEglrQRDELIEE-KQRMQQKIDTMT 455
Cdd:PRK00409 510 LIGEDKEKlnELIaslEELERELEQKAEEAEALLKEAEKLK---EELEEKKEKLQE---EEDKLLEEaEKEAQQAIKEAK 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 456 KEVFDLQETLLWKDKKIGALEKQKEYIACLR--NERDMLREELADL----QETVKTGEKhglVIIPDGTPNGDVshepva 529
Cdd:PRK00409 584 KEADEIIKELRQLQKGGYASVKAHELIEARKrlNKANEKKEKKKKKqkekQEELKVGDE---VKYLSLGQKGEV------ 654
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 578806708 530 gaITVVSQEAAQVLesagEGPLDVR-----LRKLAGEKEELLSQIRKLKLQL 576
Cdd:PRK00409 655 --LSIPDDKEAIVQ----AGIMKMKvplsdLEKIQKPKKKKKKKPKTVKPKP 700
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
323-695 |
9.05e-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: 42.50 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 323 DTSLSEL-RDIYDLKDQIQDVEGRYMQGLKELKESLSEVE--EKYKKAMVSNA-QLDNEKNNLIYQVDTLKDVIEEQEEQ 398
Cdd:pfam10174 239 DTKISSLeRNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEvyKSHSKFMKNKIdQLKQELSKKESELLALQTKLETLTNQ 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 399 MAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEK----QRMQQKIDTMTKEVFDLQETLLWKDKKIGA 474
Cdd:pfam10174 319 NSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKtkqlQDLTEEKSTLAGEIRDLKDMLDVKERKINV 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 475 LEKQKEyiaclrNERDMLRE---ELADLQETVKTGEKHglviipdgTPNGDVSHEPVAGAITvvsqEAAQVLEsagegpl 551
Cdd:pfam10174 399 LQKKIE------NLQEQLRDkdkQLAGLKERVKSLQTD--------SSNTDTALTTLEEALS----EKERIIE------- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 552 dvRLRK-LAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDlaglQNGSdlqFIEMQRDANRQISEYKFKLSKAEQDIT 630
Cdd:pfam10174 454 --RLKEqREREDRERLEELESLKKENKDLKEKVSALQPELTE----KESS---LIDLKEHASSLASSGLKKDSKLKSLEI 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 631 TLEQSI---SRLEGQVLRYKTAAENAEKVED-------------ELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEK 694
Cdd:pfam10174 525 AVEQKKeecSKLENQLKKAHNAEEAVRTNPEindrirlleqevaRYKEESGKAQAEVERLLGILREVENEKNDKDKKIAE 604
|
.
gi 578806708 695 M 695
Cdd:pfam10174 605 L 605
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
606-697 |
9.89e-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: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 606 EMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKtaAENA-------------EKVEDELKAEKRKLQRELR 672
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE--AEVEeleaeleekderiERLERELSEARSEERREIR 462
|
90 100 110
....*....|....*....|....*....|....*...
gi 578806708 673 -----TALD--------KIEEMEMTNSHLAKRLEKMKA 697
Cdd:COG2433 463 kdreiSRLDreierlerELEEERERIEELKRKLERLKE 500
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
323-669 |
1.23e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 323 DTSLSELRDIYDLKDQIQDVEGRY---MQGLKELKESLSEVEEKYKKAmvsNAQLDNEKNNLIYQvdtlkdvieEQEEQm 399
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDYQAA---SDHLNLVQTALRQQ---------EKIER- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 400 aefYREN-EEKSKELERQkhmcsvlqhkMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIG----- 473
Cdd:PRK04863 353 ---YQADlEELEERLEEQ----------NEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIqyqqa 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 474 --ALEKQK--------------EYIACLRNERDMLREELADLQETVKtgekhglviipdgtpngdvshepvagaitvVSQ 537
Cdd:PRK04863 420 vqALERAKqlcglpdltadnaeDWLEEFQAKEQEATEELLSLEQKLS------------------------------VAQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 538 EAAQVLESAGEgpldvRLRKLAGE--KEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQngsdlQFIEMQRDANRQI 615
Cdd:PRK04863 470 AAHSQFEQAYQ-----LVRKIAGEvsRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELE-----QRLRQQQRAERLL 539
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 578806708 616 SEYKFKLSKAEQDITTLEQSISRLEGQVLRYK----TAAENAEKVEDELKAEKRKLQR 669
Cdd:PRK04863 540 AEFCKRLGKNLDDEDELEQLQEELEARLESLSesvsEARERRMALRQQLEQLQARIQR 597
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
373-696 |
1.25e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 373 QLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSvlqhkmEELKEGLRQRDELIEEKQRMQqkiD 452
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN------SELTEARTERDQFSQESGNLD---D 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 453 TMTKEVFDLQetllwKDKKIGALEKQKEYIACLRNER-----DMLREELADLQETVKTGEkhGLVIIPDGTPNGDVSHEP 527
Cdd:pfam15921 378 QLQKLLADLH-----KREKELSLEKEQNKRLWDRDTGnsitiDHLRRELDDRNMEVQRLE--ALLKAMKSECQGQMERQM 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 528 VA-----GAITVVSQEAAQvLESAGEGPLDVrLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDL 602
Cdd:pfam15921 451 AAiqgknESLEKVSSLTAQ-LESTKEMLRKV-VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 603 QFIEMQ---------RDANRQISEYKFKLSKAEQDITTLEQSI---SRLEGQVLRyKTAAENAEKVEDELKAEKRKLQ-R 669
Cdd:pfam15921 529 KLQELQhlknegdhlRNVQTECEALKLQMAEKDKVIEILRQQIenmTQLVGQHGR-TAGAMQVEKAQLEKEINDRRLElQ 607
|
330 340 350
....*....|....*....|....*....|.
gi 578806708 670 ELRTALD----KIEEMEMTNSHLakRLEKMK 696
Cdd:pfam15921 608 EFKILKDkkdaKIRELEARVSDL--ELEKVK 636
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
334-501 |
2.03e-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: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 334 DLKDQIQDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 413
Cdd:COG4942 24 EAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 414 ERQKHMCSVL------QHKMEELKEGLRQRD--ELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEYIACL 485
Cdd:COG4942 100 EAQKEELAELlralyrLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170
....*....|....*.
gi 578806708 486 RNERDMLREELADLQE 501
Cdd:COG4942 180 LAELEEERAALEALKA 195
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
350-683 |
2.14e-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: 41.25 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 350 LKELKESLSEVEEKYKKamvsnaqldnEKNNLIYQVDTLKDVIEEQEEQMAEF---YRENEEKSKELERQKHMCSvlqhk 426
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKK----------EINDKEKQVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQD----- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 427 mEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEyiaclrnerdmlreelADLQETVKTG 506
Cdd:pfam05483 282 -ENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKE----------------AQMEELNKAK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 507 EKHGLVIipdgtpngdVSHEPVAGAITVVSQEAAQVLESAGE--GPLDVRLRKLAGEKEELLSQIRKLKLQLEE------ 578
Cdd:pfam05483 345 AAHSFVV---------TEFEATTCSLEELLRTEQQRLEKNEDqlKIITMELQKKSSELEEMTKFKNNKEVELEElkkila 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 579 ERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKaeqdITTLEQSISRlegQVLRYKTAAENAEKVED 658
Cdd:pfam05483 416 EDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTA----IKTSEEHYLK---EVEDLKTELEKEKLKNI 488
|
330 340
....*....|....*....|....*
gi 578806708 659 ELKAEKRKLQRELRTALDKIEEMEM 683
Cdd:pfam05483 489 ELTAHCDKLLLENKELTQEASDMTL 513
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
392-697 |
2.17e-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: 41.25 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 392 IEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKK 471
Cdd:pfam05483 372 LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 472 IGALEKQKEYIAC-----LRNERDMLRE-ELADLQETVKTGEKHGLVIipdgtPNGDVSHEPVAGAITVVSQEAAQVLES 545
Cdd:pfam05483 452 IHDLEIQLTAIKTseehyLKEVEDLKTElEKEKLKNIELTAHCDKLLL-----ENKELTQEASDMTLELKKHQEDIINCK 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 546 AGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQ--KCSRNDGTvgdlaglQNGSDLQFIEMQRDANRQISEYkfKLS 623
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDevKCKLDKSE-------ENARSIEYEVLKKEKQMKILEN--KCN 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 624 KAEQDITTLEQSISRL--EGQVLRYKTAAENAE---------KVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRL 692
Cdd:pfam05483 598 NLKKQIENKNKNIEELhqENKALKKKGSAENKQlnayeikvnKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEV 677
|
....*
gi 578806708 693 EKMKA 697
Cdd:pfam05483 678 EKAKA 682
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
330-662 |
2.76e-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: 41.21 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 330 RDIYDLKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVsnaQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFyrENEEK 409
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL---RVKEKIGELEAEIASLERSIAEKERELEDA--EERLA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 410 SKELERQKhmcsvLQHKMEELKEGL----RQRDELIEEKQRMQQKIDTMTKEVFDLQETL-LWKDKkigaLEKQKEYIAC 484
Cdd:TIGR02169 326 KLEAEIDK-----LLAEIEELEREIeeerKRRDKLTEEYAELKEELEDLRAELEEVDKEFaETRDE----LKDYREKLEK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 485 LRNERDMLREELADLQETVKTGEKHGLVIipdgtpngdvshepvagaitvvsQEAAQVLESagegpldvRLRKLAGEKEE 564
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADL-----------------------NAAIAGIEA--------KINELEEEKED 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 565 LLSQIRKLKLQLEeerqkcsrndgtvgdlaglqngsdlQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVL 644
Cdd:TIGR02169 446 KALEIKKQEWKLE-------------------------QLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAR 500
|
330
....*....|....*...
gi 578806708 645 RYKTAAENAEKVEDELKA 662
Cdd:TIGR02169 501 ASEERVRGGRAVEEVLKA 518
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
382-688 |
2.79e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 382 IYQVDTLKDVIEEQEEQMAE------FYRENEEKSKELERQkhmCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMT 455
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEhqmelkYLKQYKEKACEIRDQ---ITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 456 KEVFDLQETllwkdkkIGALEKQKEyiaclrnERDMLREELADLQETVKTGEKHGLviipdgtpnGDVSHEPVAgaiTVV 535
Cdd:TIGR00606 262 SKIMKLDNE-------IKALKSRKK-------QMEKDNSELELKMEKVFQGTDEQL---------NDLYHNHQR---TVR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 536 SQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDlagLQNGSDLQFIEMQRDANRQI 615
Cdd:TIGR00606 316 EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS---LATRLELDGFERGPFSERQI 392
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578806708 616 SEY-KFKLSKAEQDITTLEQSISRLEGQVlryKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHL 688
Cdd:TIGR00606 393 KNFhTLVIERQEDEAKTAAQLCADLQSKE---RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL 463
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
551-706 |
2.86e-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: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 551 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCS-------RNDGTVGDLAGLQNGSDLQ-FIE-------MQRDANRQI 615
Cdd:COG3883 56 LQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralyRSGGSVSYLDVLLGSESFSdFLDrlsalskIADADADLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 616 SEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKM 695
Cdd:COG3883 136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
170
....*....|.
gi 578806708 696 KANRTALLAQQ 706
Cdd:COG3883 216 AAAAAAAAAAA 226
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
554-699 |
2.92e-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: 39.91 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 554 RLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVG------DLAGLQngSDLQFIEMQR-DANRQISEYKFKLSKAE 626
Cdd:COG1579 46 RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnkEYEALQ--KEIESLKRRIsDLEDEILELMERIEELE 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806708 627 QDITTLEQSISRLEGQVLRYKTAAENAEKvedELKAEKRKLQRELRTALDKIEEmemtnsHLAKRLEKMKANR 699
Cdd:COG1579 124 EELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEAEREELAAKIPP------ELLALYERIRKRK 187
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
350-676 |
2.96e-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: 40.93 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 350 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLiyqvdtlkdviEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKME- 428
Cdd:pfam01576 14 LQKVKERQQKAESELKELEKKHQQLCEEKNAL-----------QEQLQAETELCAEAEEMRARLAARKQELEEILHELEs 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 429 ELKEGLRQRDELIEEKQRMQQKIDTMTKEVFD-------LQETLLWKDKKIGALEKQ----KEYIACLRNERDMLREELA 497
Cdd:pfam01576 83 RLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEeeaarqkLQLEKVTTEAKIKKLEEDilllEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 498 DLQETVKTGEKHGLVIIPDGTpngdvSHEPVagaitVVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLE 577
Cdd:pfam01576 163 EFTSNLAEEEEKAKSLSKLKN-----KHEAM-----ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 578 EERQKCSRNDgtvgdlaglqngsdlqfiEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVE 657
Cdd:pfam01576 233 ELRAQLAKKE------------------EELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQR 294
|
330
....*....|....*....
gi 578806708 658 DELKAEKRKLQRELRTALD 676
Cdd:pfam01576 295 RDLGEELEALKTELEDTLD 313
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
327-508 |
2.97e-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: 40.77 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 327 SELRDIYDLKDQIQDVEGRYM----------QGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQ-------VDTLK 389
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQnqeklnqqkdEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkeliIKNLD 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 390 DVIEEQEEQMAEFYRE-------NEEKSKELERQKHMCSVLQHKMEELKEGL----RQRDELIE-------EKQRMQQKI 451
Cdd:TIGR04523 461 NTRESLETQLKVLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVkdltKKISSLKEkieklesEKKEKESKI 540
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 578806708 452 DTMTKEVFDLQETLLWKDKKIGALEKQKEyIACLRNERDMLREELADLQETVKTGEK 508
Cdd:TIGR04523 541 SDLEDELNKDDFELKKENLEKEIDEKNKE-IEELKQTQKSLKKKQEEKQELIDQKEK 596
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
328-702 |
3.20e-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: 40.80 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 328 ELRDIYDLKDQIQDVEGRyMQGLKELKESLSEVEEKYKKAMvSNAQLDNEKNNLIY----QVDTLKDVIEEQEEqmaefy 403
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGS-SDRILELDQELRKAERELSKAE-KNSLTETLKKEVKSlqneKADLDRKLRKLDQE------ 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 404 reNEEKSKELERQKHMCSVLQHKMEE----LKEGLRQRDELIEE------KQRMQQKIDTMTKEVFDLQETLLWKDKKIG 473
Cdd:TIGR00606 524 --MEQLNHHTTTRTQMEMLTKDKMDKdeqiRKIKSRHSDELTSLlgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELA 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 474 ALEKQKEYIaclRNERDMLREELADLQETV-----KTGEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVL-ESAG 547
Cdd:TIGR00606 602 SLEQNKNHI---NNELESKEEQLSSYEDKLfdvcgSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTdENQS 678
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 548 EGPLDVRLRKLAGEKEELLSQIR--------KLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQ------RDANR 613
Cdd:TIGR00606 679 CCPVCQRVFQTEAELQEFISDLQsklrlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPelrnklQKVNR 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 614 QISEYKFKLSKAEQ-----------------DITTLEQSISRLEGQVLRYKTAAENAEKVE-----DELKAEKRKLQREL 671
Cdd:TIGR00606 759 DIQRLKNDIEEQETllgtimpeeesakvcltDVTIMERFQMELKDVERKIAQQAAKLQGSDldrtvQQVNQEKQEKQHEL 838
|
410 420 430
....*....|....*....|....*....|.
gi 578806708 672 RTALDKIEEMEMTNSHLAKRLEKMKANRTAL 702
Cdd:TIGR00606 839 DTVVSKIELNRKLIQDQQEQIQHLKSKTNEL 869
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
388-465 |
4.45e-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: 4.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578806708 388 LKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKeglRQRDELIEEKQRMQQKIDTMTKEVFDLQETL 465
Cdd:pfam05266 100 LKDRQTKLLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELE---RQLALAKEKKEAADKEIARLKSEAEKLEQEI 174
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
347-432 |
5.39e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 39.33 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 347 MQGLKELKESLSEVEEKYKkamvsnaQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHK 426
Cdd:COG4026 127 IPEYNELREELLELKEKID-------EIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSR 199
|
....*.
gi 578806708 427 MEELKE 432
Cdd:COG4026 200 FEELLK 205
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
323-582 |
6.16e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 323 DTSLSELRD-----IYDLKDQIQDVEGR----YMQGLKELKESLSEVEEKYKKAmvsnaqldnEKNNLIYQVDTLKDVIE 393
Cdd:PRK05771 19 DEVLEALHElgvvhIEDLKEELSNERLRklrsLLTKLSEALDKLRSYLPKLNPL---------REEKKKVSVKSLEELIK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 394 EQEEQMAEFYRENEEKSKELErqkhmcsvlqhkmeelkeglrqrdELIEEKQRMQQKIDTMTK-EVFDLQETLLWKDKKI 472
Cdd:PRK05771 90 DVEEELEKIEKEIKELEEEIS------------------------ELENEIKELEQEIERLEPwGNFDLDLSLLLGFKYV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 473 ----GALEKQKEyiaclrnERDMLREELADLQETVKTGEKHGLVIIPDgtpngdvshepvAGAITVVSQEAAQV----LE 544
Cdd:PRK05771 146 svfvGTVPEDKL-------EELKLESDVENVEYISTDKGYVYVVVVVL------------KELSDEVEEELKKLgferLE 206
|
250 260 270
....*....|....*....|....*....|....*...
gi 578806708 545 SAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQK 582
Cdd:PRK05771 207 LEEEGTPSELIREIKEELEEIEKERESLLEELKELAKK 244
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
387-509 |
7.53e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.46 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 387 TLKDVIEEQEEqmaefyrenEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQrmqqkidtmtKEVFDLQETLL 466
Cdd:COG2433 377 SIEEALEELIE---------KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELE 437
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 578806708 467 WKDKKIGALE------KQKEY--------IACLRNERDMLREELADLQETVKTGEKH 509
Cdd:COG2433 438 EKDERIERLErelseaRSEERreirkdreISRLDREIERLERELEEERERIEELKRK 494
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
346-699 |
7.63e-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: 39.57 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 346 YMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQH 425
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 426 KMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETllWKDKKIGALEKQKEYIACLRNERDMLREELADLQETVKT 505
Cdd:pfam02463 248 DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE--ELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 506 GEKHglviipdgtpngdvshepvagaitvVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQ--KC 583
Cdd:pfam02463 326 AEKE-------------------------LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLakKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 584 SRNDGTVGDLAGL-QNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKA 662
Cdd:pfam02463 381 LESERLSSAAKLKeEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350
....*....|....*....|....*....|....*..
gi 578806708 663 EKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANR 699
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEE 497
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
328-669 |
8.06e-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: 39.57 E-value: 8.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 328 ELRDIYDLKDQIQDVEGRYMQGLKELKES------LSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDV-----IEEQE 396
Cdd:TIGR00618 227 ELKHLREALQQTQQSHAYLTQKREAQEEQlkkqqlLKQLRARIEELRAQEAVLEETQERINRARKAAPLAahikaVTQIE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 397 EQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKID--TMTKEVFDLQETLLwkdKKIGA 474
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEvaTSIREISCQQHTLT---QHIHT 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 475 LEKQKEYIACLRNERDMLREELADLQETVKTgekhglviiPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEG----- 549
Cdd:TIGR00618 384 LQQQKTTLTQKLQSLCKELDILQREQATIDT---------RTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCtaqce 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 550 ----PLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKcsrndgtvgdlaglqngsDLQFIEMQRDANRQISEYKFKLSKA 625
Cdd:TIGR00618 455 klekIHLQESAQSLKEREQQLQTKEQIHLQETRKKAV------------------VLARLLELQEEPCPLCGSCIHPNPA 516
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 578806708 626 EQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQR 669
Cdd:TIGR00618 517 RQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRAS 560
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
330-505 |
9.24e-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: 39.07 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 330 RDIYDLKDQIQDVEGRY---MQGLKELKESLSEVEEKYKKAMVSNAQLDNE--KNNLIY--QVDTLKDVIEEQEEQMAEF 402
Cdd:pfam06160 86 KALDEIEELLDDIEEDIkqiLEELDELLESEEKNREEVEELKDKYRELRKTllANRFSYgpAIDELEKQLAEIEEEFSQF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 403 YRENE-----EKSKELERQKHMCSVLQHKMEELKEGLRQ-RDELIEEKQRMQQKIDTMTKEVFDLQETLLwkDKKIGALE 476
Cdd:pfam06160 166 EELTEsgdylEAREVLEKLEEETDALEELMEDIPPLYEElKTELPDQLEELKEGYREMEEEGYALEHLNV--DKEIQQLE 243
|
170 180 190
....*....|....*....|....*....|.
gi 578806708 477 KQ-KEYIACLRN-ERDMLREELADLQETVKT 505
Cdd:pfam06160 244 EQlEENLALLENlELDEAEEALEEIEERIDQ 274
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
404-701 |
9.37e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 38.74 E-value: 9.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 404 RENEEKSKELERQKhmcSVLQHKMEELKEglrQRDELIEEKQRMQQKIDTMTKEVFDLQEtllwkdkKIGALEKQK---- 479
Cdd:COG1340 4 DELSSSLEELEEKI---EELREEIEELKE---KRDELNEELKELAEKRDELNAQVKELRE-------EAQELREKRdeln 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 480 EYIACLRNERDMLREELADLQETVKTGEKHGLVIIPDGTPngdvshepvagaITVVSQEAAQVLESAGEGPLDVrlrkla 559
Cdd:COG1340 71 EKVKELKEERDELNEKLNELREELDELRKELAELNKAGGS------------IDKLRKEIERLEWRQQTEVLSP------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 560 gEKE-ELLSQIRKLKLQLEEERQKCSRNDgtvgDLAGLQNGSDLQFIEMqRDANRQISEYKFKLSKAEQDITTLEQSISR 638
Cdd:COG1340 133 -EEEkELVEKIKELEKELEKAKKALEKNE----KLKELRAELKELRKEA-EEIHKKIKELAEEAQELHEEMIELYKEADE 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806708 639 LEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTA 701
Cdd:COG1340 207 LRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKA 269
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
350-510 |
9.67e-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: 39.26 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 350 LKELKESLSEVEEKYKKAMvsnAQLDNEKNNLIYQvdTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEE 429
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQA---AKLQGSDLDRTVQ--QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806708 430 LKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALE--------KQKEYIACLRNERDMLREELADLQE 501
Cdd:TIGR00606 869 LKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLEtflekdqqEKEELISSKETSNKKAQDKVNDIKE 948
|
....*....
gi 578806708 502 TVKtgEKHG 510
Cdd:TIGR00606 949 KVK--NIHG 955
|
|
| |
