|
Name |
Accession |
Description |
Interval |
E-value |
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
220-574 |
3.42e-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: 313.17 E-value: 3.42e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 220 LDEKSDKQYAENYT---------RPSSRNSASATTPLSGNSSRRGSGDTSSLIDPDTSLSELRDiydlkdqiqdvegrym 290
Cdd:pfam09738 30 VEENADRVFDMSSSsgadtasgsPTASTTSAGTLNSLGGTSSRRSSEDSSISLEDEGSLRDIKH---------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 291 qglkelkeSLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKM 370
Cdd:pfam09738 94 --------ELKEVEEKYRKAMISNAQLDNEKSNLMYQVDLLKDKLEEMEESLAELQRELREKNKELERLKRNLRRLQFQL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 371 EELKEGLRQRDELIeekqrmqqkidtmtkevfdlqetllwkdkkigalekqkeyiaclrnerdmlreeladlqetvktgE 450
Cdd:pfam09738 166 AELKEQLKQRDELI-----------------------------------------------------------------E 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 451 KHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQ-KCSRN 529
Cdd:pfam09738 181 KHGLVIVPDENTNGEEENSPADAKRALVSVEAAEVLESAGEGSLDVRLKKLADEKEELLDEVRKLKLQLEEEKSkRNSTR 260
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 578806728 530 DGTVGDLAGLQNGSDLqfIEMQRDANRQISEYKFKLSKAEQDITT 574
Cdd:pfam09738 261 SSQSPDGFGLENGSHV--IEVQREANKQISDYKFKLQKAEQEITT 303
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
247-625 |
4.00e-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: 66.63 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 247 LSGNSSRRGSGDTSSLIDPDTSLSELRDIYDLKDQ---IQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNN 323
Cdd:TIGR02169 655 MTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRElssLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 324 LIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQrdELIEEKQRMQQKIDtmtKEVFD 403
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLE---EEVSR 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 404 LQETLLWKDKKIGALEKQKEYiacLRNERDMLREELADLQETVKTGEKhglviipdgtpNGDVSHEPVAGAITVVSQEAA 483
Cdd:TIGR02169 810 IEARLREIEQKLNRLTLEKEY---LEKEIQELQEQRIDLKEQIKSIEK-----------EIENLNGKKEELEEELEELEA 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 484 QVLEsagegpLDVRLRKLAGEKEELLSQIRKLKL---QLEEERQKCSRNDGTVGDLAGLQNGsDLQFIEMQRDANRQISE 560
Cdd:TIGR02169 876 ALRD------LESRLGDLKKERDELEAQLRELERkieELEAQIEKKRKRLSELKAKLEALEE-ELSEIEDPKGEDEEIPE 948
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578806728 561 YKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEME 625
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
293-624 |
1.85e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 293 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEE 372
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 373 LKEglrQRDELIEEKQRMQQKIDTMTKEVFDLQETLlwkDKKIGALEKQKEYIACLRNERDMLREELADLQETVKTGEKh 452
Cdd:TIGR02168 759 LEA---EIEELEERLEEAEEELAEAEAEIEELEAQI---EQLKEELKALREALDELRAELTLLNEEAANLRERLESLER- 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 453 glviipdgtpngdvSHEPVAGAITVVSQEAAQVLEsagegpldvRLRKLAGEKEELLSQIRKLKLQLEE-ERQKCSRNDG 531
Cdd:TIGR02168 832 --------------RIAATERRLEDLEEQIEELSE---------DIESLAAEIEELEELIEELESELEAlLNERASLEEA 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 532 TVGDLAGLQN-GSDLQFIEMQR-DANRQISEYKFKLSKAEQDITTLEQSISRLEGQVL-RYKTAAENAEKVEDELKAEKR 608
Cdd:TIGR02168 889 LALLRSELEElSEELRELESKRsELRRELEELREKLAQLELRLEGLEVRIDNLQERLSeEYSLTLEEAEALENKIEDDEE 968
|
330
....*....|....*.
gi 578806728 609 KLQRELRTALDKIEEM 624
Cdd:TIGR02168 969 EARRRLKRLENKIKEL 984
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
254-624 |
2.72e-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: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 254 RGSGDTSSLIdpdtsLSELRDIYDLKDQIQDVEGRYMQGLKELKESLSEVEEkYKKAMVSNAQLDNEKNNLIYQVDTLKD 333
Cdd:TIGR02168 663 GGSAKTNSSI-----LERRREIEELEEKIEELEEKIAELEKALAELRKELEE-LEEELEQLRKELEELSRQISALRKDLA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 334 VIEEQEEQMAEFYRENEEKSKELERQKhmcSVLQHKMEELKEGLrqrDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDK 413
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEI---EELEERLEEAEEEL---AEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 414 KIGALE----KQKEYIACLRNERDMLREELADLQETVKTGEKHGLVI---IPDGTPNGDVSHEPVAGAITVV-SQEAAQV 485
Cdd:TIGR02168 811 ELTLLNeeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEALLNERaSLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 486 LESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLagLQNGSDLQFIEMQrDANRQISEYKFKL 565
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL--QERLSEEYSLTLE-EAEALENKIEDDE 967
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 566 SKAEQDITTLEQSISRLeGQV-LRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEM 624
Cdd:TIGR02168 968 EEARRRLKRLENKIKEL-GPVnLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
293-625 |
1.20e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 293 LKELKESL------SEVEEKYKkamvsnaQLDNEKNNLiyQVDTLKDVIEEQEEQMAEF---YRENEEKSKELERQKHMc 363
Cdd:TIGR02168 195 LNELERQLkslerqAEKAERYK-------ELKAELREL--ELALLVLRLEELREELEELqeeLKEAEEELEELTAELQE- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 364 svLQHKMEELKEGLRQRDELIEEKQR----MQQKIDTMTKEVFDLQETLLWKDKKIGALEkqkEYIACLRNERDMLREEL 439
Cdd:TIGR02168 265 --LEEKLEELRLEVSELEEEIEELQKelyaLANEISRLEQQKQILRERLANLERQLEELE---AQLEELESKLDELAEEL 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 440 ADLQETVKTGEKhglviipdgtpngdvSHEPVAGAITvVSQEAAQVLESAGEGpLDVRLRKLAGEKEELLSQIRKLKLQL 519
Cdd:TIGR02168 340 AELEEKLEELKE---------------ELESLEAELE-ELEAELEELESRLEE-LEEQLETLRSKVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 520 EEERQKCSRNDGTVGdlaglqngsdlQFIEMQRDANRQISEYKFKLSKAEqdITTLEQSISRLEGQVLRYKTAAENAEKV 599
Cdd:TIGR02168 403 ERLEARLERLEDRRE-----------RLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEALEELREE 469
|
330 340
....*....|....*....|....*.
gi 578806728 600 EDELKAEKRKLQRELRTALDKIEEME 625
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLE 495
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
347-596 |
2.76e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 347 RENEEKSKELERQkhmcsvLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQkeyIA 426
Cdd:COG4942 23 AEAEAELEQLQQE------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE---IA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 427 CLRNERDMLREELAD-LQETVKTGEKHGL-VIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEgpldvRLRKLAGE 504
Cdd:COG4942 94 ELRAELEAQKEELAElLRALYRLGRQPPLaLLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA-----ELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 505 KEELLSQIRKLKLQLEEERQKcsrndgtvgdLAGLQNGSDlqfiEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEG 584
Cdd:COG4942 169 LEAERAELEALLAELEEERAA----------LEALKAERQ----KLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
250
....*....|..
gi 578806728 585 QVLRYKTAAENA 596
Cdd:COG4942 235 EAAAAAERTPAA 246
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
276-451 |
1.02e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 276 YDLKDQIQDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKE 355
Cdd:TIGR02168 291 YALANEISRLEQQ----KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 356 LErqkhmcsVLQHKMEELKEGL-RQRDELIEEKQRMQQ---KIDTMTKEVFDLQETL---------LWKDKKIGALEKQK 422
Cdd:TIGR02168 367 LE-------ELESRLEELEEQLeTLRSKVAQLELQIASlnnEIERLEARLERLEDRRerlqqeieeLLKKLEEAELKELQ 439
|
170 180
....*....|....*....|....*....
gi 578806728 423 EYIACLRNERDMLREELADLQETVKTGEK 451
Cdd:TIGR02168 440 AELEELEEELEELQEELERLEEALEELRE 468
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
279-542 |
1.36e-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: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 279 KDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKN-------NLIYQVDTLKDVIEEQEEQMAEFYRENEE 351
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEelqkelyALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 352 KSKELERQKhmcSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQ----KEYIAC 427
Cdd:TIGR02168 321 LEAQLEELE---SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqlELQIAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 428 LRNERDMLREELADLQETVktgEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEgpLDVRLRKLAGEKEE 507
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRR---ERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELER--LEEALEELREELEE 472
|
250 260 270
....*....|....*....|....*....|....*
gi 578806728 508 LLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNG 542
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
277-640 |
1.38e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 277 DLKDQIQDVE--------GRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEF 345
Cdd:PRK02224 191 QLKAQIEEKEekdlherlNGLESELAELDEEIERYEEQREQARETRDEADevlEEHEERREELETLEAEIEDLRETIAET 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 346 YRENEEKSKELERQKHMCSVLqhkmEELKEGLRQRDELIE-EKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEy 424
Cdd:PRK02224 271 EREREELAEEVRDLRERLEEL----EEERDDLLAEAGLDDaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAE- 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 425 iaCLRNERDMLREELADLQETVKTGEKhglviipdGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGPldVRLRKLAGE 504
Cdd:PRK02224 346 --SLREDADDLEERAEELREEAAELES--------ELEEAREAVEDRREEIEELEEEIEELRERFGDAP--VDLGNAEDF 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 505 KEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDL----QFIEMQRDANRqISEYKFKLSKAEQDITTLEQSIS 580
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpecgQPVEGSPHVET-IEEDRERVEELEAELEDLEEEVE 492
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806728 581 RLEGQVLRYKTAAENAEKVEDelKAEKRKLQRELR-TALDKIEEMEMTNSHLAKRLEKMKA 640
Cdd:PRK02224 493 EVEERLERAEDLVEAEDRIER--LEERREDLEELIaERRETIEEKRERAEELRERAAELEA 551
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
327-640 |
1.40e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 327 QVDTLKDVIEEQEEQMAEFYRENEEKSKELErqkhmcsvLQHKMEELK--EGLRQRDELIEEKQRMQQKIDTMTKEVFDL 404
Cdd:TIGR02169 185 NIERLDLIIDEKRQQLERLRREREKAERYQA--------LLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 405 QETLLWKDKKIGALEKQKEYIAclRNERDMLREELADLQETVktGEKHGLViipdgtpngdvshEPVAGAITVVSQEAAQ 484
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKI--GELEAEI-------------ASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 485 vlesagegpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNG--SDLQFIEMQRDANRQ-ISEY 561
Cdd:TIGR02169 320 ---------AEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDlrAELEEVDKEFAETRDeLKDY 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806728 562 KFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 640
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
331-649 |
1.79e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 331 LKDVIEEQEEQM---------AEFYRENEEKSKELERQkhmcsVLQHKMEELKEGLRQRDELIEEKQRMQQKIDtmtkev 401
Cdd:COG1196 191 LEDILGELERQLeplerqaekAERYRELKEELKELEAE-----LLLLKLRELEAELEELEAELEELEAELEELE------ 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 402 fdlqetllwkdKKIGALEKQKEYiacLRNERDMLREELADLQEtvktgekhglviipdgtpngdvshepvagAITVVSQE 481
Cdd:COG1196 260 -----------AELAELEAELEE---LRLELEELELELEEAQA-----------------------------EEYELLAE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 482 AAQvlESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQkcsrndgtvgdlaglqngsdlqfiemqrdanrQISEY 561
Cdd:COG1196 297 LAR--LEQDIARLEERRRELEERLEELEEELAELEEELEELEE--------------------------------ELEEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 562 KFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKAN 641
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
....*...
gi 578806728 642 RTALLAQQ 649
Cdd:COG1196 423 LEELEEAL 430
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
274-493 |
2.53e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 274 DIYDLKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLD---NEKNNLIYQVDTLKDVIEEQEEQMAEFYRENE 350
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEalqAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 351 EKSKE----------------LERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETllwKDKK 414
Cdd:COG3883 97 RSGGSvsyldvllgsesfsdfLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA---KAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806728 415 IGALEKQKEYIACLRNERDMLREELADLQETVKTGEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGP 493
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
277-640 |
3.00e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 277 DLKDQIQDVEGRYMQGLKELKESLSEVE---------EKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYR 347
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISSELPelreeleklEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 348 ENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQEtllwkdkKIGALEKQKEYIAC 427
Cdd:PRK03918 270 ELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE-------RIKELEEKEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 428 LRNERDMLREELADLQETVKTGEKhglviipdgtpngdvshepvAGAITVVSQEAAQVLESAGEGPLDVRLRKLAGEKEE 507
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYEE--------------------AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 508 LLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQI-SEYKFKLSKAEQDITTLEQSISRL---- 582
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELlEEYTAELKRIEKELKEIEEKERKLrkel 482
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 578806728 583 ---------EGQVLRYKTAAENAEKVEDELKA----EKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 640
Cdd:PRK03918 483 relekvlkkESELIKLKELAEQLKELEEKLKKynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE 553
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
494-648 |
4.52e-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: 45.30 E-value: 4.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 494 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAglqngSDLQFIEMQ-RDANRQISEYKFKLSKA---- 568
Cdd:COG1579 15 LDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLE-----KEIKRLELEiEEVEARIKKYEEQLGNVrnnk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 569 -----EQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEmtnSHLAKRLEKMKANRT 643
Cdd:COG1579 90 eyealQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEEL---AELEAELEELEAERE 166
|
....*
gi 578806728 644 ALLAQ 648
Cdd:COG1579 167 ELAAK 171
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
269-649 |
5.21e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 269 LSELRDIYDLKDQIQDVEGRYmqglKELKESLSEVEEKYKKAMVSNAQLDNEKNNLiyqvdtlkdvieEQEEQMAEFYRE 348
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEY----AELQEELEELEEELEELEAELEELREELEKL------------EKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 349 NEEKSKELERqkhmcsvLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKigALEKQKEYIACL 428
Cdd:COG4717 134 LEALEAELAE-------LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE--ELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 429 RNERDMLREELADLQETVKTGEKH----------------------------GLVIIPDGTPNGDVSHEPVAGAITVV-- 478
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEEleqleneleaaaleerlkearlllliaaALLALLGLGGSLLSLILTIAGVLFLVlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 479 ---------SQEAAQVLESAGEGPLDVRLRKLagEKEELLSQIRKLKL-------QLEEERQKCSRNDGTVGDLAGLQNG 542
Cdd:COG4717 285 llallflllAREKASLGKEAEELQALPALEEL--EEEELEELLAALGLppdlspeELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 543 SDLQFIEMQRDAN------------RQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAEnaekvEDELKAEKRKL 610
Cdd:COG4717 363 LQLEELEQEIAALlaeagvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALD-----EEELEEELEEL 437
|
410 420 430
....*....|....*....|....*....|....*....
gi 578806728 611 QRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 649
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEEDGELAELLQ 476
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
343-626 |
5.31e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 343 AEFYRENEEKSKELERQKHMCSVLQHKMEELKEglrQRDELIEEKQRmQQKIDTMTKEVFDLQETLLWKDKKigALEKQK 422
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREK-AERYQALLKEKREYEGYELLKEKE--ALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 423 EYIaclRNERDMLREELADLQETVKTGEKHglviipdgtpngdvshepVAGAITVVSQEAAQVLESAGEGPLDVR--LRK 500
Cdd:TIGR02169 240 EAI---ERQLASLEEELEKLTEEISELEKR------------------LEEIEQLLEELNKKIKDLGEEEQLRVKekIGE 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 501 LAGEKEELLSQIRKLKLQLE----EERQKCSRNDGTVGDLAGLQngSDLQFIEMQRDA-NRQISEYKFKLSKAEQDITTL 575
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEdaeeRLAKLEAEIDKLLAEIEELE--REIEEERKRRDKlTEEYAELKEELEDLRAELEEV 376
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 578806728 576 EQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEM 626
Cdd:TIGR02169 377 DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
273-648 |
6.04e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 273 RDIYDLKDQIQDVEgrymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQM-------AEF 345
Cdd:TIGR02168 316 RQLEELEAQLEELE----SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLetlrskvAQL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 346 YRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQR--MQQKIDTMTKEVFDLQETLlwkDKKIGALEKQKE 423
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELkeLQAELEELEEELEELQEEL---ERLEEALEELRE 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 424 YIACLRNERDMLREELA-----------------DLQETVKTGEKHGLVIIPDGTPNGD-VSHEP------------VAG 473
Cdd:TIGR02168 469 ELEEAEQALDAAERELAqlqarldslerlqenleGFSEGVKALLKNQSGLSGILGVLSElISVDEgyeaaieaalggRLQ 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 474 AITVVSQEAA----QVLESAGEG-----PLDV-RLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAG----- 538
Cdd:TIGR02168 549 AVVVENLNAAkkaiAFLKQNELGrvtflPLDSiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGgvlvv 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 539 --LQNGSDLQ--------FIEMQ--------------RDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAE 594
Cdd:TIGR02168 629 ddLDNALELAkklrpgyrIVTLDgdlvrpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELE 708
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 578806728 595 NAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 648
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
427-649 |
7.41e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 427 CLRNERDMLREELADLQETVKTGEKhglviipdgtpngdvshepvagAITVVSQEAAQVLEsagegpldvRLRKLAGEKE 506
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEK----------------------ALAELRKELEELEE---------ELEQLRKELE 722
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 507 ELLSQIRKLKLQLEEERQKCSRndgtVGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQV 586
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQ----LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806728 587 LRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQQ 649
Cdd:TIGR02168 799 KALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEI 861
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
494-640 |
8.70e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 8.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 494 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCsrnDGTVGDLAGlQNGSDLQFIEMQ-RDANRQISEYKFKLSKAEQDI 572
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREEL---DELEAQIRG-NGGDRLEQLEREiERLERELEERERRRARLEALL 368
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 578806728 573 TTLEQSI-----------SRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 640
Cdd:COG4913 369 AALGLPLpasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRD 447
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
277-451 |
1.03e-04 |
|
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: 45.27 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 277 DLKDQIQDVEgrymQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 356
Cdd:pfam07888 77 ELESRVAELK----EELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETEL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 357 ERQKhmcsvlqhkmEELKEGLRQRDELIEEKQRMQQKIDTMTKEV----FDLQETLLWKDKKIGALEKQKEYIACLRN-- 430
Cdd:pfam07888 153 ERMK----------ERAKKAGAQRKEEEAERKQLQAKLQQTEEELrslsKEFQELRNSLAQRDTQVLQLQDTITTLTQkl 222
|
170 180
....*....|....*....|....*....
gi 578806728 431 --------ERDMLREELADLQETVKTGEK 451
Cdd:pfam07888 223 ttahrkeaENEALLEELRSLQERLNASER 251
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
271-642 |
1.16e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 271 ELRDIYDLKDQIQDVEGRymqgLKELKESLSEVEEK---YKKAMVSNAQLDNEKNNL-IYQVDTLKDVIEEQEEQMAEFY 346
Cdd:PRK03918 329 RIKELEEKEERLEELKKK----LKELEKRLEELEERhelYEEAKAKKEELERLKKRLtGLTPEKLEKELEELEKAKEEIE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 347 RENEEKSKELERQKHMCSVLQHKMEELKEGLRQ----RDELIEEKQrmQQKIDTMTKEVFDLQETLLWKDKKIGALEKQK 422
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKEL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 423 EYI-ACLRNERDMLR-EELAD-LQETVKTGEKHGLVIIPDGTPNGDVSHEPVAGaitvVSQEAAQVLESAGEG-PLDVRL 498
Cdd:PRK03918 483 RELeKVLKKESELIKlKELAEqLKELEEKLKKYNLEELEKKAEEYEKLKEKLIK----LKGEIKSLKKELEKLeELKKKL 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 499 RKLAGEKEELLSQIRKLKLQLEEERQKCSRN-DGTVGDLAGLQNgsdlQFIEMqRDANRQISEYKFKLSKAEQDITTLEQ 577
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGFESVEElEERLKELEPFYN----EYLEL-KDAEKELEREEKELKKLEEELDKAFE 633
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 578 SISRLEGQVLRYKTAAENAEKVEDE-----LKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANR 642
Cdd:PRK03918 634 ELAETEKRLEELRKELEELEKKYSEeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEEL 703
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
482-649 |
1.52e-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: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 482 AAQVLESAGEG--PLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNgsdlQFIEMQRDANRQIS 559
Cdd:TIGR02168 230 LVLRLEELREEleELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY----ALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 560 EYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMK 639
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
|
170
....*....|
gi 578806728 640 ANRTALLAQQ 649
Cdd:TIGR02168 386 SKVAQLELQI 395
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
335-645 |
1.62e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 335 IEEQEEQMAEFYRENEEKSKELER------QKHMCSVLQHKMEELK--EGLRQRDELIEEKQRMQQKIDTMTKEVFDLQE 406
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERlrrereKAERYQALLKEKREYEgyELLKEKEALERQKEAIERQLASLEEELEKLTE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 407 TLLWKDKKIGALEKQKEYIAclRNERDMLREELADLQETVK--TGEKHGLV-IIPDGTPNGDVSHEPVAGAITVVSQEAA 483
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELN--KKIKDLGEEEQLRVKEKIGelEAEIASLErSIAEKERELEDAEERLAKLEAEIDKLLA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 484 QVLESAGE-GPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKcsrNDGTVGDLAGLQNGSDlQFIEMQRDANRQISEYK 562
Cdd:TIGR02169 337 EIEELEREiEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE---FAETRDELKDYREKLE-KLKREINELKRELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 563 FKLSKAEQDITTLEQSISRLEGQVLRYKTAAENA----EKVEDELK---AEKRKLQRELRTALDKIEEMEMTNSHLAKRL 635
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKaleiKKQEWKLEqlaADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
330
....*....|
gi 578806728 636 EKMKANRTAL 645
Cdd:TIGR02169 493 AEAEAQARAS 502
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
274-645 |
2.62e-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: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 274 DIYDLKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEK---NNLIYQVDTLKDVIEEQEEQMAEFYRENE 350
Cdd:TIGR04523 69 KINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKeqkNKLEVELNKLEKQKKENKKNIDKFLTEIK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 351 EKSKELERQKHMCSVLQHKMEELKEglrQRDELIEEKQRMQQKIDTMTKEVFDLQETLL---WKDKKIGALEKQ----KE 423
Cdd:TIGR04523 149 KKEKELEKLNNKYNDLKKQKEELEN---ELNLLEKEKLNIQKNIDKIKNKLLKLELLLSnlkKKIQKNKSLESQiselKK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 424 YIACLRNERDMLREELADLQETVKTGEKHGLVIIPDGTPNGDVSHEP---VAGAITVVSQEAAQVLEsagegpLDVRLRK 500
Cdd:TIGR04523 226 QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKqkeLEQNNKKIKELEKQLNQ------LKSEISD 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 501 LAGEKE-----ELLSQIRKLKLQLEEERQKCSRNDGTVGDLaglqnGSDLQFIEMQRD--------ANRQISEYKFKLSK 567
Cdd:TIGR04523 300 LNNQKEqdwnkELKSELKNQEKKLEEIQNQISQNNKIISQL-----NEQISQLKKELTnsesenseKQRELEEKQNEIEK 374
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578806728 568 AEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTAL 645
Cdd:TIGR04523 375 LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
418-645 |
3.21e-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: 43.89 E-value: 3.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 418 LEKQKEYIACLRNERDMLREELADLQETVKTGEKHGLviipdgtpngDVSHEPVAGAITVVSQEAAQVLESAGEGPLDVR 497
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQLRKELE----------ELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 498 LRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQ----------ISEYKFKLSK 567
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLneeaanlrerLESLERRIAA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 568 AEQDITTLEQSISRLEGQVLRY----KTAAENAEKVEDELKA---EKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKA 640
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLaaeiEELEELIEELESELEAllnERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
....*
gi 578806728 641 NRTAL 645
Cdd:TIGR02168 916 ELEEL 920
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
293-619 |
3.46e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 293 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQM----AEFYRENEEKSKELERQKHMCSVLQH 368
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAELARLEQDIARLEERRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 369 KMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLlwKDKKIGALEKQKEYIACLRNERDMLREELADLQEtvkt 448
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL--AEAEEALLEAEAELAEAEEELEELAEELLEALRA---- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 449 gekhglviipdgtpngdvshepvagaitvVSQEAAQVLEsagegpLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSR 528
Cdd:COG1196 395 -----------------------------AAELAAQLEE------LEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 529 NDGTVGDLAGLQNGSDLQfiemQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAE-KVEDELKAEK 607
Cdd:COG1196 440 EEEALEEAAEEEAELEEE----EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgFLEGVKAALL 515
|
330
....*....|..
gi 578806728 608 RKLQRELRTALD 619
Cdd:COG1196 516 LAGLRGLAGAVA 527
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
274-623 |
4.18e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 274 DIYDLKDQIQDVEGRymqgLKELKESLSEVEE--KYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEE 351
Cdd:PRK03918 260 KIRELEERIEELKKE----IEELEEKVKELKElkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 352 KSKELERQKHMCSVLQHKMEELKEGLRQRDE---LIEEKQRMQQKIDTMTKEVFdlqetllwkDKKIGALEKQKEYIacl 428
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELYEEakaKKEELERLKKRLTGLTPEKL---------EKELEELEKAKEEI--- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 429 RNERDMLREELADLQETVKTGEKhglVIIPDGTPNGDVshePVAGAiTVVSQEAAQVLESAGEGPLDVR--LRKLAGEKE 506
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKK---AIEELKKAKGKC---PVCGR-ELTEEHRKELLEEYTAELKRIEkeLKEIEEKER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 507 ELLSQIRKLKLQLEEERqKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQV 586
Cdd:PRK03918 477 KLRKELRELEKVLKKES-ELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELK 555
|
330 340 350
....*....|....*....|....*....|....*..
gi 578806728 587 LRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEE 623
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELEELGFESVEELEE 592
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
291-632 |
4.98e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 291 QGLKELKESLSEVEEKykkamvsnaqldneKNNLIYQVDTLKDVIEEQEEQMAE----FYRENEEKSK---ELERQKHM- 362
Cdd:pfam10174 324 QHIEVLKESLTAKEQR--------------AAILQTEVDALRLRLEEKESFLNKktkqLQDLTEEKSTlagEIRDLKDMl 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 363 ------CSVLQHKMEELKEGLRQRDELIEEKQR----MQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEYI-ACLRNE 431
Cdd:pfam10174 390 dvkerkINVLQKKIENLQEQLRDKDKQLAGLKErvksLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREdRERLEE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 432 RDMLREELADLQETVKTGEKHGL----VIIPDGTPNGDVSHEPVAGAITVVSQEAAQVLESAGEGPLDVRLRKL------ 501
Cdd:pfam10174 470 LESLKKENKDLKEKVSALQPELTekesSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAhnaeea 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 502 AGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGL-------QNGSDLQFIEMQRDANRQISEykfkLSKAEQDITT 574
Cdd:pfam10174 550 VRTNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGIlreveneKNDKDKKIAELESLTLRQMKE----QNKKVANIKH 625
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 575 LEQSISRLEGQVLryktaaENAEKVEDELKAEKRKLQ-RELRTALDKI-EEMEMTNSHLA 632
Cdd:pfam10174 626 GQQEMKKKGAQLL------EEARRREDNLADNSQQLQlEELMGALEKTrQELDATKARLS 679
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
494-648 |
5.20e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 494 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNdGTVGDLAGLQNGSDLQFIEMQRDANRQISEYKfklskaEQDIT 573
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRL-GRQPPLALLLSPEDFLDAVRRLQYLKYLAPAR------REQAE 153
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578806728 574 TLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMKANRTALLAQ 648
Cdd:COG4942 154 ELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
300-638 |
5.49e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 300 LSEVEEKYKKAMVSNAQLDNEKNNL---IYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEG 376
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLekfIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 377 LRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQ-----------KEYIAcLRNERDMLREELADLQET 445
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKvkelkelkekaEEYIK-LSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 446 vktgekhglviipdgtpngdvshepvagaITVVSQEAAQVLESAGEGPLDV-RLRKLAGEKEELLSQIRKLK---LQLEE 521
Cdd:PRK03918 316 -----------------------------LSRLEEEINGIEERIKELEEKEeRLEELKKKLKELEKRLEELEerhELYEE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 522 ERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQISEykfKLSKAEQDITTLEQSISRLEGQVLRYKTAAE-----NA 596
Cdd:PRK03918 367 AKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEE---EISKITARIGELKKEIKELKKAIEELKKAKGkcpvcGR 443
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 578806728 597 EKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKM 638
Cdd:PRK03918 444 ELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELREL 485
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
278-649 |
6.02e-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: 43.09 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 278 LKDQIQDVEGRYMQGL-KELKESLSEVEEKYKkamvsnaQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 356
Cdd:TIGR04523 293 LKSEISDLNNQKEQDWnKELKSELKNQEKKLE-------EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 357 ERqkhmcsvlqhKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEYiacLRNERDMLR 436
Cdd:TIGR04523 366 EE----------KQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKEL---LEKEIERLK 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 437 EELADLQETVKTGEKhglviipdgtpngdvshepvagaitvvsQEAAqvlesagegpLDVRLRKLAGEKEELLSQIRKLK 516
Cdd:TIGR04523 433 ETIIKNNSEIKDLTN----------------------------QDSV----------KELIIKNLDNTRESLETQLKVLS 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 517 LQLEEERQKCSRNdgtvgdlaglqngsdlqfiemqrdanrqiseyKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENA 596
Cdd:TIGR04523 475 RSINKIKQNLEQK--------------------------------QKELKSKEKELKKLNEEKKELEEKVKDLTKKISSL 522
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 578806728 597 EKVEDELKAEKRKLQRELRTALDKIEEMEMTN---------SHLAKRLEKMKANRTALLAQQ 649
Cdd:TIGR04523 523 KEKIEKLESEKKEKESKISDLEDELNKDDFELkkenlekeiDEKNKEIEELKQTQKSLKKKQ 584
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
277-625 |
6.96e-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: 42.70 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 277 DLKDQIQDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 356
Cdd:TIGR04523 311 ELKSELKNQEKK----LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 357 ERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDtmtKEVFDLQETLLWKDKKIGALEKQ----KEYIACLRNER 432
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE---KEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTR 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 433 DMLREELADLQETVKTgEKHGLviipdgtpngdvshEPVAGAITVVSQEAAQVLESAGEgpLDVRLRKLAGEKEELLSQI 512
Cdd:TIGR04523 464 ESLETQLKVLSRSINK-IKQNL--------------EQKQKELKSKEKELKKLNEEKKE--LEEKVKDLTKKISSLKEKI 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 513 RKLKLQLEEERQKCSRNDgtvGDLAGLQNGSDLQFIEMQRDA-NRQISEYKF-------KLSKAEQDITTLEQSISRLEG 584
Cdd:TIGR04523 527 EKLESEKKEKESKISDLE---DELNKDDFELKKENLEKEIDEkNKEIEELKQtqkslkkKQEEKQELIDQKEKEKKDLIK 603
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 578806728 585 QVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEME 625
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
549-640 |
8.34e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 8.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 549 EMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRYKtaAENA-------------EKVEDELKAEKRKLQRELR 615
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE--AEVEeleaeleekderiERLERELSEARSEERREIR 462
|
90 100 110
....*....|....*....|....*....|....*...
gi 578806728 616 -----TALD--------KIEEMEMTNSHLAKRLEKMKA 640
Cdd:COG2433 463 kdreiSRLDreierlerELEEERERIEELKRKLERLKE 500
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
269-401 |
8.91e-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: 41.45 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 269 LSELRDIYD-LKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQ-----VDTLKDVIEEQEEQM 342
Cdd:COG1579 33 LAELEDELAaLEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEalqkeIESLKRRISDLEDEI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 343 AEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQR-DELIEEKQRMQQKIDTMTKEV 401
Cdd:COG1579 113 LELMERIEELEEELAELEAELAELEAELEEKKAELDEElAELEAELEELEAEREELAAKI 172
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
273-451 |
1.11e-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: 42.36 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 273 RDIYDLKDQIQDVEGRYMQGLKELKESLSEVEE---KYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYREN 349
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEElerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 350 EEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEkqrMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEYIAclr 429
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELAD---LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA--- 461
|
170 180
....*....|....*....|..
gi 578806728 430 NERDMLREELADLQETVKTGEK 451
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRVEK 483
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
293-642 |
1.25e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 293 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVI------------EEQEEQMAEFYRENEEKSKELERQK 360
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgrelteEHRKELLEEYTAELKRIEKELKEIE 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 361 HMCSVLQHKMEELKEGLRQRDELIEEKQRMQQ--------------KIDTMTKEVFDLQETLLWKDKKIGALEKQKEYIA 426
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESELIKLKELAEQlkeleeklkkynleELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 427 CLRNERDMLREELADLQETVKTGEKHGLVIipdgtpnGDVSHEPVAGAItvvsqeaaQVLESAGEGPLdvRLRKLAGEKE 506
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEEL-------GFESVEELEERL--------KELEPFYNEYL--ELKDAEKELE 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 507 ELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNgsdlqfiemqrDANRQISEYKFKlsKAEQDITTLEQSISRLEGQV 586
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELE-----------ELEKKYSEEEYE--ELREEYLELSRELAGLRAEL 682
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 578806728 587 lryktaaENAEKVEDELKAEKRKLQRELRTALDKIEEMEMtnshLAKRLEKMKANR 642
Cdd:PRK03918 683 -------EELEKRREEIKKTLEKLKEELEEREKAKKELEK----LEKALERVEELR 727
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
277-448 |
1.35e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 277 DLKDQIQDVEGRY---MQGLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKS 353
Cdd:TIGR04523 465 SLETQLKVLSRSInkiKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 354 KELERQK------HMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQ-----K 422
Cdd:TIGR04523 545 DELNKDDfelkkeNLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKElekakK 624
|
170 180 190
....*....|....*....|....*....|..
gi 578806728 423 EY------IACLRNERDMLREELADLQETVKT 448
Cdd:TIGR04523 625 ENeklssiIKNIKSKKNKLKQEVKQIKETIKE 656
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
293-645 |
1.59e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.64 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 293 LKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQH---K 369
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNvqtE 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 370 MEELKEGLRQRDELIEekqRMQQKIDTMTKEVFDLQETllwkdkkIGALEKQKEYIACLRNERDMLREELADLQET--VK 447
Cdd:pfam15921 550 CEALKLQMAEKDKVIE---ILRQQIENMTQLVGQHGRT-------AGAMQVEKAQLEKEINDRRLELQEFKILKDKkdAK 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 448 TGEKHGLViipdgtpnGDVSHEPV----AG-----AITVVSQEAAQVLESAGEG---------PLDVRLRKLAGEKEELL 509
Cdd:pfam15921 620 IRELEARV--------SDLELEKVklvnAGserlrAVKDIKQERDQLLNEVKTSrnelnslseDYEVLKRNFRNKSEEME 691
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 510 SQIRKLKLQLEEERQKCSRNDGTVGDLaglqNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISrlegqvlry 589
Cdd:pfam15921 692 TTTNKLKMQLKSAQSELEQTRNTLKSM----EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMT--------- 758
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 590 ktaaeNAEKVEDELKAEKRKLQRELRT-ALDKIE---EMEMTNSHLAKRLEKMKANRTAL 645
Cdd:pfam15921 759 -----NANKEKHFLKEEKNKLSQELSTvATEKNKmagELEVLRSQERRLKEKVANMEVAL 813
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
325-425 |
1.61e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 325 IYQVDTLK--DVI---EEQEEQMAEFYRENEEKSKELERQKhmcSVLQHKMEELKEglrQRDELIEE-KQRMQQKIDTMT 398
Cdd:PRK00409 510 LIGEDKEKlnELIaslEELERELEQKAEEAEALLKEAEKLK---EELEEKKEKLQE---EEDKLLEEaEKEAQQAIKEAK 583
|
90 100
....*....|....*....|....*..
gi 578806728 399 KEVFDLQETLLWKDKKIGALEKQKEYI 425
Cdd:PRK00409 584 KEADEIIKELRQLQKGGYASVKAHELI 610
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
344-639 |
1.73e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 344 EFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETllwkDKKIGALEKQKE 423
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL----KEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 424 YiacLRNERDMLREELADLQETVKTGEKHglviipdgtpngdvshepvagaITVVSQEAAQVLESAGEGPLDVRLRKLAG 503
Cdd:PRK03918 249 S---LEGSKRKLEEKIRELEERIEELKKE----------------------IEELEEKVKELKELKEKAEEYIKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 504 EKEELLSQIRKLKLQLEEERQKCSRNdgtvgdlaglqngsdlqfIEMQRDANRQISEYKFKLSKAEQDITTLE------Q 577
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEINGIEER------------------IKELEEKEERLEELKKKLKELEKRLEELEerhelyE 365
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578806728 578 SISRLEGQVLRYKT--AAENAEKVEDELK-AEKRK--LQRELRTALDKIEEMEMTNSHLAKRLEKMK 639
Cdd:PRK03918 366 EAKAKKEELERLKKrlTGLTPEKLEKELEeLEKAKeeIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
281-636 |
2.18e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.31 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 281 QIQDVEGRYMQGLKELKESLsEVEEKYKKAMVSNAQ-LDNEKNNLIYQVDTLkdvieEQEEQmaefyrENEEKSKELERQ 359
Cdd:pfam01576 346 QLQEMRQKHTQALEELTEQL-EQAKRNKANLEKAKQaLESENAELQAELRTL-----QQAKQ------DSEHKRKKLEGQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 360 khmcsvLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKE---------------- 423
Cdd:pfam01576 414 ------LQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQdtqellqeetrqklnl 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 424 --YIACLRNERDMLREELADLQETVKTGEKHGLviipdgtpngdvSHEPVAGAITVVSQEAAQVLESAGEGpldvrlrkl 501
Cdd:pfam01576 488 stRLRQLEDERNSLQEQLEEEEEAKRNVERQLS------------TLQAQLSDMKKKLEEDAGTLEALEEG--------- 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 502 ageKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGlqngsDLQFIEMQRDANRQIseykfkLSKAEQDITTLEQSISR 581
Cdd:pfam01576 547 ---KKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ-----ELDDLLVDLDHQRQL------VSNLEKKQKKFDQMLAE 612
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 578806728 582 LEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLE 636
Cdd:pfam01576 613 EKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEME 667
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
266-612 |
2.69e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 266 DTSLSELRDIYDLKDQIQDVEGRY---MQGLKELKESLSEVEEKYKKAmvsNAQLDNEKNNLIYQvdtlkdvieEQEEQm 342
Cdd:PRK04863 286 EEALELRRELYTSRRQLAAEQYRLvemARELAELNEAESDLEQDYQAA---SDHLNLVQTALRQQ---------EKIER- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 343 aefYREN-EEKSKELERQkhmcsvlqhkMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIG----- 416
Cdd:PRK04863 353 ---YQADlEELEERLEEQ----------NEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIqyqqa 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 417 --ALEKQK--------------EYIACLRNERDMLREELADLQETVKtgekhglviipdgtpngdvshepvagaitvVSQ 480
Cdd:PRK04863 420 vqALERAKqlcglpdltadnaeDWLEEFQAKEQEATEELLSLEQKLS------------------------------VAQ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 481 EAAQVLESAGEgpldvRLRKLAGE--KEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQngsdlQFIEMQRDANRQI 558
Cdd:PRK04863 470 AAHSQFEQAYQ-----LVRKIAGEvsRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELE-----QRLRQQQRAERLL 539
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 578806728 559 SEYKFKLSKAEQDITTLEQSISRLEGQVLRYK----TAAENAEKVEDELKAEKRKLQR 612
Cdd:PRK04863 540 AEFCKRLGKNLDDEDELEQLQEELEARLESLSesvsEARERRMALRQQLEQLQARIQR 597
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
316-639 |
3.48e-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: 40.49 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 316 QLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSvlqhkmEELKEGLRQRDELIEEKQRMQqkiD 395
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAN------SELTEARTERDQFSQESGNLD---D 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 396 TMTKEVFDLQetllwKDKKIGALEKQKEYIACLRNER-----DMLREELADLQETVKTGEkhGLVIIPDGTPNGDVSHEP 470
Cdd:pfam15921 378 QLQKLLADLH-----KREKELSLEKEQNKRLWDRDTGnsitiDHLRRELDDRNMEVQRLE--ALLKAMKSECQGQMERQM 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 471 VA-----GAITVVSQEAAQvLESAGEGPLDVrLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDL 545
Cdd:pfam15921 451 AAiqgknESLEKVSSLTAQ-LESTKEMLRKV-VEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 546 QFIEMQ---------RDANRQISEYKFKLSKAEQDITTLEQSI---SRLEGQVLRyKTAAENAEKVEDELKAEKRKLQ-R 612
Cdd:pfam15921 529 KLQELQhlknegdhlRNVQTECEALKLQMAEKDKVIEILRQQIenmTQLVGQHGR-TAGAMQVEKAQLEKEINDRRLElQ 607
|
330 340 350
....*....|....*....|....*....|.
gi 578806728 613 ELRTALD----KIEEMEMTNSHLakRLEKMK 639
Cdd:pfam15921 608 EFKILKDkkdaKIRELEARVSDL--ELEKVK 636
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
266-447 |
3.95e-03 |
|
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: 40.58 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 266 DTSLSEL-RDIYDLKDQIQDVEGRYMQGLKELKESLSEVE--EKYKKAMVSNA-QLDNEKNNLIYQVDTLKDVIEEQEEQ 341
Cdd:pfam10174 239 DTKISSLeRNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEvyKSHSKFMKNKIdQLKQELSKKESELLALQTKLETLTNQ 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 342 MAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEK----QRMQQKIDTMTKEVFDLQETLLWKDKKIGA 417
Cdd:pfam10174 319 NSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKtkqlQDLTEEKSTLAGEIRDLKDMLDVKERKINV 398
|
170 180 190
....*....|....*....|....*....|...
gi 578806728 418 LEKQKEyiaclrNERDMLRE---ELADLQETVK 447
Cdd:pfam10174 399 LQKKIE------NLQEQLRDkdkQLAGLKERVK 425
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
277-444 |
4.17e-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: 39.75 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 277 DLKDQIQDVEGRymqgLKELKESLSEVEEKYKKAMVSNAQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKEL 356
Cdd:COG4942 24 EAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 357 ERQKHMCSVL------QHKMEELKEGLRQRD--ELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQKEYIACL 428
Cdd:COG4942 100 EAQKEELAELlralyrLGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170
....*....|....*.
gi 578806728 429 RNERDMLREELADLQE 444
Cdd:COG4942 180 LAELEEERAALEALKA 195
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
494-649 |
4.53e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 494 LDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCS-------RNDGTVGDLAGLQNGSDLQ-FIE-------MQRDANRQI 558
Cdd:COG3883 56 LQAELEALQAEIDKLQAEIAEAEAEIEERREELGeraralyRSGGSVSYLDVLLGSESFSdFLDrlsalskIADADADLL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 559 SEYKFKLSKAEQDITTLEQSISRLEGQVLRYKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKM 638
Cdd:COG3883 136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
170
....*....|.
gi 578806728 639 KANRTALLAQQ 649
Cdd:COG3883 216 AAAAAAAAAAA 226
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
273-605 |
5.48e-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: 40.05 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 273 RDIYDLKDQIQDVEGRYMQGLKELKESLSEVEEKYKKAMVsnaQLDNEKNNLIYQVDTLKDVIEEQEEQMaefyRENEEK 352
Cdd:TIGR02169 251 EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQL---RVKEKIGELEAEIASLERSIAEKEREL----EDAEER 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 353 SKELErqkhmcsvlqhkmEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEKQkeyIACLRNER 432
Cdd:TIGR02169 324 LAKLE-------------AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE---FAETRDEL 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 433 DMLREELADLQETVktgekhglviipdgtpngdvshepvagaitvvsqeaaqvlesageGPLDVRLRKLAGEKEELLSQI 512
Cdd:TIGR02169 388 KDYREKLEKLKREI---------------------------------------------NELKRELDRLQEELQRLSEEL 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 513 RKLKLQLEEERQKCSRNDGTVGDLA---GLQNGSDLQFIEMQRDANRQISEYKFKLSKAEQDITTLEQSISRLEGQVLRY 589
Cdd:TIGR02169 423 ADLNAAIAGIEAKINELEEEKEDKAleiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARAS 502
|
330
....*....|....*.
gi 578806728 590 KTAAENAEKVEDELKA 605
Cdd:TIGR02169 503 EERVRGGRAVEEVLKA 518
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
266-525 |
5.53e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.91 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 266 DTSLSELRD-----IYDLKDQIQDVEGR----YMQGLKELKESLSEVEEKYKKAmvsnaqldnEKNNLIYQVDTLKDVIE 336
Cdd:PRK05771 19 DEVLEALHElgvvhIEDLKEELSNERLRklrsLLTKLSEALDKLRSYLPKLNPL---------REEKKKVSVKSLEELIK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 337 EQEEQMAEFYRENEEKSKELErqkhmcsvlqhkmeelkeglrqrdELIEEKQRMQQKIDTMTK-EVFDLQETLLWKDKKI 415
Cdd:PRK05771 90 DVEEELEKIEKEIKELEEEIS------------------------ELENEIKELEQEIERLEPwGNFDLDLSLLLGFKYV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 416 ----GALEKQKEyiaclrnERDMLREELADLQETVKTGEKHGLVIIPDgtpngdvshepvAGAITVVSQEAAQV----LE 487
Cdd:PRK05771 146 svfvGTVPEDKL-------EELKLESDVENVEYISTDKGYVYVVVVVL------------KELSDEVEEELKKLgferLE 206
|
250 260 270
....*....|....*....|....*....|....*...
gi 578806728 488 SAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQK 525
Cdd:PRK05771 207 LEEEGTPSELIREIKEELEEIEKERESLLEELKELAKK 244
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
290-375 |
5.91e-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: 5.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 290 MQGLKELKESLSEVEEKYKkamvsnaQLDNEKNNLIYQVDTLKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHK 369
Cdd:COG4026 127 IPEYNELREELLELKEKID-------EIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSR 199
|
....*.
gi 578806728 370 MEELKE 375
Cdd:COG4026 200 FEELLK 205
|
|
| DUF724 |
pfam05266 |
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ... |
331-408 |
6.05e-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: 38.41 E-value: 6.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578806728 331 LKDVIEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKeglRQRDELIEEKQRMQQKIDTMTKEVFDLQETL 408
Cdd:pfam05266 100 LKDRQTKLLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELE---RQLALAKEKKEAADKEIARLKSEAEKLEQEI 174
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
330-452 |
6.16e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 6.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 330 TLKDVIEEQEEqmaefyrenEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQrmqqkidtmtKEVFDLQETLL 409
Cdd:COG2433 377 SIEEALEELIE---------KELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLE----------AEVEELEAELE 437
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 578806728 410 WKDKKIGALE------KQKEY--------IACLRNERDMLREELADLQETVKTGEKH 452
Cdd:COG2433 438 EKDERIERLErelseaRSEERreirkdreISRLDREIERLERELEEERERIEELKRK 494
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
325-631 |
6.73e-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: 39.64 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 325 IYQVDTLKDVIEEQEEQMAE------FYRENEEKSKELERQkhmCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMT 398
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEhqmelkYLKQYKEKACEIRDQ---ITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 399 KEVFDLQETllwkdkkIGALEKQKEyiaclrnERDMLREELADLQETVKTGEKHGLviipdgtpnGDVSHEPVAgaiTVV 478
Cdd:TIGR00606 262 SKIMKLDNE-------IKALKSRKK-------QMEKDNSELELKMEKVFQGTDEQL---------NDLYHNHQR---TVR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 479 SQEAAQVLESAGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDlagLQNGSDLQFIEMQRDANRQI 558
Cdd:TIGR00606 316 EKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQS---LATRLELDGFERGPFSERQI 392
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578806728 559 SEY-KFKLSKAEQDITTLEQSISRLEGQVlryKTAAENAEKVEDELKAEKRKLQRELRTALDKIEEMEMTNSHL 631
Cdd:TIGR00606 393 KNFhTLVIERQEDEAKTAAQLCADLQSKE---RLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKEL 463
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
335-640 |
7.16e-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: 39.70 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 335 IEEQEEQMAEFYRENEEKSKELERQKHMCSVLQHKMEELKEGLRQRDELIEEKQRMQQKIDTMTKEVFDLQETLLWKDKK 414
Cdd:pfam05483 372 LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 415 IGALEKQKEYIAC-----LRNERDMLRE-ELADLQETVKTGEKHGLVIipdgtPNGDVSHEPVAGAITVVSQEAAQVLES 488
Cdd:pfam05483 452 IHDLEIQLTAIKTseehyLKEVEDLKTElEKEKLKNIELTAHCDKLLL-----ENKELTQEASDMTLELKKHQEDIINCK 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 489 AGEGPLDVRLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQRDANRQISEYKFKLSKA 568
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENK 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 569 EQDITTLEQsisrlEGQVLRYKTAAENAE---------KVEDELKAEKRKLQRELRTALDKIEEMEMTNSHLAKRLEKMK 639
Cdd:pfam05483 607 NKNIEELHQ-----ENKALKKKGSAENKQlnayeikvnKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAK 681
|
.
gi 578806728 640 A 640
Cdd:pfam05483 682 A 682
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
271-645 |
8.76e-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: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 271 ELRDIYDLKDQIQDVEGRyMQGLKELKESLSEVEEKYKKAMvSNAQLDNEKNNLIYqvdtLKDVIEEQEEQMAEFYRENE 350
Cdd:TIGR00606 452 KQEELKFVIKELQQLEGS-SDRILELDQELRKAERELSKAE-KNSLTETLKKEVKS----LQNEKADLDRKLRKLDQEME 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 351 EKSKELERQKHMCSVLQHKMEE----LKEGLRQRDELIEE------KQRMQQKIDTMTKEVFDLQETLLWKDKKIGALEK 420
Cdd:TIGR00606 526 QLNHHTTTRTQMEMLTKDKMDKdeqiRKIKSRHSDELTSLlgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQ 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 421 QKEYIaclRNERDMLREELADLQETV-----KTGEKHGLVIIPDGTPNGDVSHEPVAGAITVVSQEAAQVL-ESAGEGPL 494
Cdd:TIGR00606 606 NKNHI---NNELESKEEQLSSYEDKLfdvcgSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTdENQSCCPV 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 495 DVRLRKLAGEKEELLSQIR--------KLKLQLEEERQKCSRNDGTVGDLAGLQNGSDLQFIEMQ------RDANRQISE 560
Cdd:TIGR00606 683 CQRVFQTEAELQEFISDLQsklrlapdKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPelrnklQKVNRDIQR 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 561 YKFKLSKAEQ-----------------DITTLEQSISRLEGQVLRYKTAAENAEKVE-----DELKAEKRKLQRELRTAL 618
Cdd:TIGR00606 763 LKNDIEEQETllgtimpeeesakvcltDVTIMERFQMELKDVERKIAQQAAKLQGSDldrtvQQVNQEKQEKQHELDTVV 842
|
410 420
....*....|....*....|....*..
gi 578806728 619 DKIEEMEMTNSHLAKRLEKMKANRTAL 645
Cdd:TIGR00606 843 SKIELNRKLIQDQQEQIQHLKSKTNEL 869
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
497-642 |
9.06e-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: 38.37 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578806728 497 RLRKLAGEKEELLSQIRKLKLQLEEERQKCSRNDGTVG------DLAGLQngSDLQFIEMQR-DANRQISEYKFKLSKAE 569
Cdd:COG1579 46 RLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvrnnkEYEALQ--KEIESLKRRIsDLEDEILELMERIEELE 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 578806728 570 QDITTLEQSISRLEGQVLRYKTAAENAEKvedELKAEKRKLQRELRTALDKIEEmemtnsHLAKRLEKMKANR 642
Cdd:COG1579 124 EELAELEAELAELEAELEEKKAELDEELA---ELEAELEELEAEREELAAKIPP------ELLALYERIRKRK 187
|
|
| |
