|
Name |
Accession |
Description |
Interval |
E-value |
| CASP_C |
pfam08172 |
CASP C terminal; This domain is the C-terminal region of the CASP family of proteins. It is a ... |
423-643 |
7.10e-67 |
|
CASP C terminal; This domain is the C-terminal region of the CASP family of proteins. It is a Golgi membrane protein which is thought to have a role in vesicle transport.
Pssm-ID: 462392 [Multi-domain] Cd Length: 247 Bit Score: 219.85 E-value: 7.10e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 423 ELQVRITEAVATATEQRELIARLEQDLSIIQSIQR--PDAEGAAEHRLEKIPEPIKEATAlfyGPAA-----PASGALPE 495
Cdd:pfam08172 1 TLQEELSSLNAELEEQQELNAKLENDLLKVQDEASnaFSFNDASSAGSGVSRYPPSGGRR---SPTSsiisgFEPSESSS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 496 GQVDSLLSIISSQRERFRARNQELEAENRLAQHTLQALQSELDSLRADNIKLFEKIKFLQSYPGRGSGSDDTEL------ 569
Cdd:pfam08172 78 SSDSSILPIVTSQRDRFRQRNAELEEELRKQFETISSLRQEIASLQKDNLKLYEKTRYLQSYNRGGGGGTKSSSstsssa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 570 ----------------RYSSQYEERLDPFSSFSKRERQRKYLSLSPWDKATLSMGRLVLSNKMARTIGFFYTLFLHCLVF 633
Cdd:pfam08172 158 saygnnpnpsdvealdKYRKAYEESLNPFAAFRGRESERAYKRLSPLERLVLSLTRLVLANRTSRNLFFFYCLALHLLVF 237
|
250
....*....|
gi 31652236 634 LVLYKLAWSE 643
Cdd:pfam08172 238 FTLYYVSNSS 247
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-542 |
4.68e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 18 QQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTpedlrkqvaplLKSFQGEIDALSKRSKEAEAAFLNVYKRLi 97
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAE-----------LEELEAELAELEAELEELRLELEELELEL- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 98 dvpdpvpaLDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQ 177
Cdd:COG1196 284 --------EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 178 kLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVA 257
Cdd:COG1196 356 -AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 258 QREAETLREQLSSANHSLQLASQIQKapdveqaievltrssLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQIsQ 337
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEA---------------LLELLAELLEEAALLEAALAELLEELAEAAARLLLLL-E 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 338 LEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAG---------TQDAAKPLEVLLLEKNRSLQSENA 408
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAaalqnivveDDEVAAAAIEYLKAAKAGRATFLP 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 409 ALRISNSDLSGRCAELQVRITEAVATATEQRELIARLEQDLSIIQSIQR-PDAEGAAEHRLEKIPEPIKEATAlfYGPAA 487
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLvAARLEAALRRAVTLAGRLREVTL--EGEGG 656
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 31652236 488 PASGALPEGQVDSLLSIISSQRERFRARNQELEAENRLAQHTLQALQSELDSLRA 542
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-411 |
1.09e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 107 DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIA--LEKEQKLQNDFA 184
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEerIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 185 EKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQRA 254
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 255 EVAQREAETLREQLSSANHSLqlasqiqkapdveqaievltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLR---ENS 331
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEI---------------------EELEELIEELESELEALLNERASLEEALALLRselEEL 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 332 ASQISQLEQQLSAKNSTLKQLEEKLkGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALR 411
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKL-AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
13-543 |
1.85e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 13 KRFDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNtpedlRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNV 92
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER-----LEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 93 YKRLidvpdpvpaLDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIA 172
Cdd:COG1196 350 EEEL---------EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 173 LEKEQKLQNDFAEKERKLQETQmsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEmimtDLERANQ 252
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEE-----ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE----ELAEAAA 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 253 RAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSA 332
Cdd:COG1196 492 RLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 333 SQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAPSE-------GAGTQDAAKPLEVLLLEKNRSLQS 405
Cdd:COG1196 572 GRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDtllgrtlVAARLEAALRRAVTLAGRLREVTL 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 406 ENAALRISNSDLSGRCAELQVRITEAVATATEQRELIARLEQDLSIIQSIQRPDAEGAAEHRLEKIPEPIKEATAlfygp 485
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL----- 726
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 31652236 486 aapasgalpEGQVDSLLSIISSQRERFRARNQELEAENRLAQHTLQALQSELDSLRAD 543
Cdd:COG1196 727 ---------EEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
111-579 |
9.89e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.79 E-value: 9.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 111 QLQLKVQRLHDIETENQKLRETLEEYNKEFAEvknQEVTIKALKEKIREYEQTLKNQAETIalekeQKLQNDFAEKERKL 190
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEE---LEAELAELEAELEELRLELEELELEL-----EEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 191 QEtqmsttskLEEAEHKVQSLQTALEKTRTELfdlktkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS 270
Cdd:COG1196 298 AR--------LEQDIARLEERRRELEERLEEL-------EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 271 ANHSLQLASQIQKApdveqaiEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLK 350
Cdd:COG1196 363 AEEALLEAEAELAE-------AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 351 QLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQ---------------DAAKPLEVLLLE--KNRSLQSENAALRIS 413
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEaalleaalaelleelAEAAARLLLLLEaeADYEGFLEGVKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 414 NSDLSGRCAELQVRITEAVATATEQRELIARLEQDlsiIQSIQRPDAEGAAEHRLEKIPEPIKEATALFYGPAAPASGAL 493
Cdd:COG1196 516 LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQN---IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 494 PEGQVDSLLSIISSQRERFRARNQELEAENRLAQHTLQALQSELDSLRADNIKLFEKIKFLQSYPGRGSGSDDTELRYSS 573
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA 672
|
....*.
gi 31652236 574 QYEERL 579
Cdd:COG1196 673 ALLEAE 678
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-334 |
4.75e-08 |
|
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: 55.54 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 105 ALDLGQQLQLKVQRLH-DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIAL--EKEQKLQN 181
Cdd:COG4942 18 QADAAAEAEAELEQLQqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEleKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 182 DFAEKERKLQET-----QMSTTSKLEEAEHKVQSLQTAlekTRTELFDLKTKYDEEttaKADEIEMIMTDLERANQRAEV 256
Cdd:COG4942 98 ELEAQKEELAELlralyRLGRQPPLALLLSPEDFLDAV---RRLQYLKYLAPARRE---QAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31652236 257 AQREAETLREQLSSANHSLQLASQIQKApdveqaievlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 334
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQK----------LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
82-408 |
5.96e-08 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 55.73 E-value: 5.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 82 SKEAEAAFLNVYKRLIDVPDPVPALdlgQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT-----IKALKEK 156
Cdd:COG5185 221 LLEKAKEIINIEEALKGFQDPESEL---EDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANnlikqFENTKEK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 157 IREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYD-EETTA 235
Cdd:COG5185 298 IAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 236 KAD-----------EIEMIMTDLERANQRAE--------VAQREAETLREQLSSANHSLQLASQIQKA-----PDVEQAI 291
Cdd:COG5185 378 ELDsfkdtiestkeSLDEIPQNQRGYAQEILatledtlkAADRQIEELQRQIEQATSSNEEVSKLLNEliselNKVMREA 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 292 EVLTRSSLEVELAAKEREIAQ----LVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEvkk 367
Cdd:COG5185 458 DEESQSRLEEAYDEINRSVRSkkedLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARG--- 534
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 31652236 368 ELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENA 408
Cdd:COG5185 535 YAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQ 575
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
127-353 |
4.14e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 127 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALekEQKLQNDFAEKERKLQETQM-STTSKLEEAE 205
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELeELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 206 HKVQSLQTALEKTRTELFDLKTKYDEettAKADEIEmimtDLERANQRAEVAQREAETLREQLSSANHSLQLAsqiqkAP 285
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRG---NGGDRLE----QLEREIERLERELEERERRRARLEALLAALGLP-----LP 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31652236 286 DVEQaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLE 353
Cdd:COG4913 377 ASAE------------EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-454 |
5.84e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 117 QRLHDIETENQKLRETLEEYNKEfaevKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQms 196
Cdd:TIGR02169 184 ENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLT-- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 197 ttsklEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQ 276
Cdd:TIGR02169 258 -----EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA------K 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 277 LASQIQKapdVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRensaSQISQLEQQLSAKNSTLKQLEEKL 356
Cdd:TIGR02169 327 LEAEIDK---LLAEIE-----ELEREIEEERKRRDKLTEEYAELKEELEDLR----AELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 357 kgqadyEEVKKELNILKsmefapsegaGTQDAakplevlLLEKNRSLQSENAALRISNSDLSGRCAELQVRITEAVATAT 436
Cdd:TIGR02169 395 ------EKLKREINELK----------RELDR-------LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451
|
330
....*....|....*...
gi 31652236 437 EQRELIARLEQDLSIIQS 454
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQ 469
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
173-457 |
7.56e-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: 52.75 E-value: 7.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 173 LEKEQKLQNDFAEKERKLQETQMS-TTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTakadEIEMIMTDLERAN 251
Cdd:TIGR02168 205 LERQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEELKEAEEELEELTAELQELEE----KLEELRLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 252 QRAEVAQREAETLREQLSSANHSLQLASqiQKAPDVEQAIEVLTRSSLEV---------ELAAKEREIAQLVEDVQRLQA 322
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILR--ERLANLERQLEELEAQLEELeskldelaeELAELEEKLEELKEELESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 323 SLTKLR---ENSASQISQLEQQLSAKNSTLKQLEEKLKG-QADYEEVKKELNILKSM-EFAPSEGAGTQDAAKPLEVLLL 397
Cdd:TIGR02168 359 ELEELEaelEELESRLEELEEQLETLRSKVAQLELQIASlNNEIERLEARLERLEDRrERLQQEIEELLKKLEEAELKEL 438
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 31652236 398 EKNRS-LQSENAALRISNSDLSGRCAELQVRITEAVATATEQRELIARLEQDLSIIQSIQR 457
Cdd:TIGR02168 439 QAELEeLEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
15-299 |
1.40e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.98 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 15 FDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAflnv 92
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELesKLDELAEELAELEEKLEELKEELESLEAELEELEAE---- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 93 ykrlidvpdpvpaldlgqqlqlkvqrLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIA 172
Cdd:TIGR02168 367 --------------------------LEELESRLEELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDRRE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 173 LEKEQKLQNDFAEKERKLQETQMSTTSK---LEEAEHKVQSLQTALEKTRTELFDLKTKYDeETTAKADEIEMIMTDLER 249
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAELEELeeeLEELQEELERLEEALEELREELEEAEQALD-AAERELAQLQARLDSLER 496
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 31652236 250 ANQRAEVAQRE-AETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSL 299
Cdd:TIGR02168 497 LQENLEGFSEGvKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRL 547
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
172-368 |
1.42e-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: 50.92 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 172 ALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERAN 251
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELE----KELAALKKEEKALLKQLAALERRIAALARRIRA----LEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 252 QRAEVAQREAETLREQLSSANHSLQLASQIQK------APDVEQAIEVLT--------RSSLEVELAAKEREIAQLVEDV 317
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPlalllsPEDFLDAVRRLQylkylapaRREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 31652236 318 QRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKE 368
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
67-375 |
3.43e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 67 LLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVpdpvpalDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ 146
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELREL-------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAE 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 147 EvtIKALKEKIREYEQTLKNQAETiaLEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQ-TALEKTRTELFDL 225
Cdd:PRK03918 526 E--YEKLKEKLIKLKGEIKSLKKE--LEKLEELKKKLAELEKKLDELE----EELAELLKELEELGfESVEELEERLKEL 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 226 KTKYDEETTAKADEIEmimtdLERANQRAEVAQREAETLREQLSSANHSLQlasqiqkapDVEQAIEVLTRSSLEVELAA 305
Cdd:PRK03918 598 EPFYNEYLELKDAEKE-----LEREEKELKKLEEELDKAFEELAETEKRLE---------ELRKELEELEKKYSEEEYEE 663
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 306 KEREIAQLVEDVQRLQAsltklrensasQISQLEQQLSAKNSTLKQLEEKLKgqaDYEEVKKELNILKSM 375
Cdd:PRK03918 664 LREEYLELSRELAGLRA-----------ELEELEKRREEIKKTLEKLKEELE---EREKAKKELEKLEKA 719
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
72-447 |
4.66e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 72 QGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYnkefaevKNQEVTIK 151
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-------RELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 152 ALKEKIREYEQTLKNQAETIALEKEQKLQnDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKtkyDE 231
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA---LE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 232 ETTAKADEIEMIMT-----------DLERANQRAEVAQ-------REAETLREQLSSANHSLQLASQIQKAPDVEQAIEV 293
Cdd:COG4717 243 ERLKEARLLLLIAAallallglggsLLSLILTIAGVLFlvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 294 LTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE-NSASQISQLEQQLS-----AKNSTLKQLEEKLKGQADYEEVKK 367
Cdd:COG4717 323 ELLAALGLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAallaeAGVEDEEELRAALEQAEEYQELKE 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 368 ELNILKSmEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSGRCAELQVRItEAVATATEQRELIARLEQ 447
Cdd:COG4717 403 ELEELEE-QLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL-EQLEEDGELAELLQELEE 480
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
110-270 |
5.98e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 110 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERK 189
Cdd:COG4913 274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 190 LQETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 269
Cdd:COG4913 354 LEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
.
gi 31652236 270 S 270
Cdd:COG4913 430 S 430
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
110-540 |
6.92e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 110 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERK 189
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAE---LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 190 LQETQMSttskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAK----ADEIEMIMTDLERANQRAEVAQREAETLR 265
Cdd:COG4717 151 LEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 266 EQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLT------KLRENSASQISQLE 339
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLallfllLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 340 QQLSAKNSTLKQLEEK-------LKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKpLEVLLLEKNRSLQSENAAlri 412
Cdd:COG4717 307 LQALPALEELEEEELEellaalgLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGVE--- 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 413 SNSDLSGRCAELQvritEAVATATEQRELIARLEQDLSIIQSIQRPDAEGAAEHRLEKIPEPIKEAtalfygpaapasga 492
Cdd:COG4717 383 DEEELRAALEQAE----EYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEEL-------------- 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 31652236 493 lpEGQVDSLLsiisSQRERFRARNQELEAENRLAQ--HTLQALQSELDSL 540
Cdd:COG4717 445 --EEELEELR----EELAELEAELEQLEEDGELAEllQELEELKAELREL 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-477 |
9.59e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 9.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 162 QTLKNQAETIALEKEQK-LQNDFAEKERKLQETQmSTTSKLEEAEHKvqsLQTALEKTRTELFDLKTKYDEEtTAKADEI 240
Cdd:TIGR02168 671 SILERRREIEELEEKIEeLEEKIAELEKALAELR-KELEELEEELEQ---LRKELEELSRQISALRKDLARL-EAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 241 EMIMTDLERANQRAEVAQREAETLREQLSSANHSL--QLASQIQKAPDVEQAIEVLTR--SSLEVELAAKEREIAQLVED 316
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAeaEIEELEAQIEQLKEELKALREalDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 317 VQRLQ---ASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQAdyEEVKKELNILKSMEFAPSEGAGTQDAAKPLE 393
Cdd:TIGR02168 826 LESLErriAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE--SELEALLNERASLEEALALLRSELEELSEEL 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 394 VLLLEKNRSLQSENAALRISNSDLSGRCAELQVRITEAVATATEQreliARLEQDLSIIQSIQRPDAEGAAEHRLEKIPE 473
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE----YSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
....
gi 31652236 474 PIKE 477
Cdd:TIGR02168 980 KIKE 983
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
232-454 |
1.22e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 232 ETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRS----SLEVELAAKE 307
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQrrleLLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 308 REIAQLVEDVQRLQASLTKLRE-----------NSASQISQLEQQLSAKNSTLKQLEEKLkgqADYEEVKKELnilksme 376
Cdd:COG4913 302 AELARLEAELERLEARLDALREeldeleaqirgNGGDRLEQLEREIERLERELEERERRR---ARLEALLAAL------- 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31652236 377 fapseGAGTQDAAKPLEVLLLEKNRSLQSENAALrisnsdlsgrcAELQVRITEAVATATEQRELIARLEQDLSIIQS 454
Cdd:COG4913 372 -----GLPLPASAEEFAALRAEAAALLEALEEEL-----------EALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
106-327 |
1.38e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 106 LDLGQQlQLKVQRLHdIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKNQAETIalekeQKLQN 181
Cdd:PHA02562 190 IDHIQQ-QIKTYNKN-IEEQRKKNGENIARKQNKYDELVEEAKTIKAeieeLTDELLNLVMDIEDPSAAL-----NKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 182 DFAEKERKLQ----ETQMST--------TSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakadeiemimtdlER 249
Cdd:PHA02562 263 AAAKIKSKIEqfqkVIKMYEkggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE--------------EI 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31652236 250 ANQRAEvAQREAETLREQLSSANHSLQLAsqIQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL 327
Cdd:PHA02562 329 MDEFNE-QSKKLLELKNKISTNKQSLITL--VDKAKKVKAAIE-----ELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
128-410 |
1.52e-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: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 128 KLRETLEEYNKEFAEVKNQEVTIKALKEKIRE--YEQTLKNQAETIALEKEQKLQNDFAEKERKLQEtqmsttsKLEEAE 205
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE-------RLEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 206 HKVQSLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLER--ANQRAEVAQREAETLREQLSSANHSLQlasqiqk 283
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLR------- 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 284 apdveqaievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS----------QISQLEQQLSAKNSTLKQLE 353
Cdd:TIGR02169 816 --------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiekeienlngKKEELEEELEELEAALRDLE 881
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 31652236 354 EKLKG-QADYEEVKKElniLKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAAL 410
Cdd:TIGR02169 882 SRLGDlKKERDELEAQ---LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
123-541 |
2.78e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 123 ETENQKLRETLEEYNKEFAEVKNQevtIKALKEKiREYEQTLKNQAETIALEKEQKLQ--NDFAEKERKLQETQMSTTSK 200
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEE---IERYEEQ-REQARETRDEADEVLEEHEERREelETLEAEIEDLRETIAETERE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 201 LEEAEHKVQSLQTALEKTRTELFDLktkydeettakADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLAsq 280
Cdd:PRK02224 274 REELAEEVRDLRERLEELEEERDDL-----------LAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAH-- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 281 iqkapdvEQAIEVLTRSSLEVELAAKE-REIAQLVEDvqRLQASLTKLREnSASQISQLEQQLSAKNSTLKQLEEKLKGQ 359
Cdd:PRK02224 341 -------NEEAESLREDADDLEERAEElREEAAELES--ELEEAREAVED-RREEIEELEEEIEELRERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 360 ADY-EEVKKELNILKSMEfapsegagtqdaaKPLEVLL------LEKNRSLQSEnaalrisnsdlsGRCAEL--QVRITE 430
Cdd:PRK02224 411 EDFlEELREERDELRERE-------------AELEATLrtarerVEEAEALLEA------------GKCPECgqPVEGSP 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 431 AVATATEQRELIARLEQDLSIIQS--------IQRPDAEGAAEHRLEKIPEPIKEATALfygpaapasgalpegqVDSLL 502
Cdd:PRK02224 466 HVETIEEDRERVEELEAELEDLEEeveeveerLERAEDLVEAEDRIERLEERREDLEEL----------------IAERR 529
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 31652236 503 SIISSQRER---FRARNQELEAENRLAQHTLQALQSELDSLR 541
Cdd:PRK02224 530 ETIEEKRERaeeLRERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
151-355 |
2.95e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 151 KALKEKIREYEQTLKNQAETIALEKEQ-KLQNDFAEKERKL-----QETQMSTTSKLEEAE-HKVQSLQT---------- 213
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKngeniARKQNKYDELVEEAKtIKAEIEELtdellnlvmd 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 214 ------ALEKTRTELFDLKTKYD-----EETTAKADEIEMIMTDLERANQRaevaqreAETLREQLSSANHSL-QLASQI 281
Cdd:PHA02562 250 iedpsaALNKLNTAAAKIKSKIEqfqkvIKMYEKGGVCPTCTQQISEGPDR-------ITKIKDKLKELQHSLeKLDTAI 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31652236 282 QKAPDVEQAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLSAKNSTLKQLEEK 355
Cdd:PHA02562 323 DELEEIMDEFNEQSKKLLELknKISTNKQSLITLVDKAKKVKAAIEELqaeFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
107-374 |
3.53e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.94 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 107 DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEfaeVKNQEVTIKALKEKIreyeQTLKNQAETIALEKEQKLQNDFAE- 185
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE---LEQNNKKIKELEKQL----NQLKSEISDLNNQKEQDWNKELKSe 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 186 ---KERKLQETQmsttSKLEEAEHKVQSLQ---TALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQraevaqr 259
Cdd:TIGR04523 316 lknQEKKLEEIQ----NQISQNNKIISQLNeqiSQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ------- 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 260 EAETLREQLSSanhslqLASQIQKAPDVEQaievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLE 339
Cdd:TIGR04523 385 EIKNLESQIND------LESKIQNQEKLNQ--------QKDEQIKKLQQEKELLEKEIERLKETIIKN----NSEIKDLT 446
|
250 260 270
....*....|....*....|....*....|....*.
gi 31652236 340 QQLSAKNSTLKQLEEKLKGQADY-EEVKKELNILKS 374
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQlKVLSRSINKIKQ 482
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
119-373 |
4.97e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.74 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 119 LHDIETENQKLRETLEEYNK---EFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQM 195
Cdd:pfam10174 201 LDQKEKENIHLREELHRRNQlqpDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVY 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 196 STTSKLeeAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQREAETLREQLSSAN 272
Cdd:pfam10174 281 KSHSKF--MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDckqHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 273 HSLQ---------------LASQIQKAPDV----EQAIEVLTR--SSLEVELAAKEREIAQLVEDVQRLQASLTklreNS 331
Cdd:pfam10174 359 SFLNkktkqlqdlteekstLAGEIRDLKDMldvkERKINVLQKkiENLQEQLRDKDKQLAGLKERVKSLQTDSS----NT 434
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 31652236 332 ASQISQLEQQLSAKNSTLKQLEEK--LKGQADYEEV---KKELNILK 373
Cdd:pfam10174 435 DTALTTLEEALSEKERIIERLKEQreREDRERLEELeslKKENKDLK 481
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
187-375 |
7.58e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 187 ERKLQETQMSTT---SKLEEAEHKVQSLQTALE--KTRTELFDLktkyDEETTAKADEIEMIMTDLERANQRAEVAQREA 261
Cdd:COG3206 167 ELRREEARKALEfleEQLPELRKELEEAEAALEefRQKNGLVDL----SEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 262 ETLREQLSSANHSL-------QLASQIQKAPDVEQAIEVLTRSSLE-----VELAAKEREI-AQLVEDVQRLQASLTKLR 328
Cdd:COG3206 243 AALRAQLGSGPDALpellqspVIQQLRAQLAELEAELAELSARYTPnhpdvIALRAQIAALrAQLQQEAQRILASLEAEL 322
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 31652236 329 ENSASQISQLEQQLSAKNSTLKQLEEKlkgQADYEEVKKELNILKSM 375
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPEL---EAELRRLEREVEVAREL 366
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
11-363 |
8.51e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.22 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 11 YWKRFDLQQLQRELDATaTVLANRQDESEQSRKRLIE---QSREFK--KNTPEDLRKQVAPLLKSFQGEIDALSKrSKEA 85
Cdd:COG5022 851 FGRSLKAKKRFSLLKKE-TIYLQSAQRVELAERQLQElkiDVKSISslKLVNLELESEIIELKKSLSSDLIENLE-FKTE 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 86 EAAFLnvyKRLIDVPDPVPALDLGQQLQLKVQRLHdieTENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK 165
Cdd:COG5022 929 LIARL---KKLLNNIDLEEGPSIEYVKLPELNKLH---EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELA 1002
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 166 N--------QAETIALEKEQK----LQNDF-------AEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLK 226
Cdd:COG5022 1003 ElskqygalQESTKQLKELPVevaeLQSASkiissesTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQ 1082
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 227 TKYDEETTAKADEIEmiMTDLERANQRAEVAQREAETLREQLSSANHslqlasQIQKAPDVEQAIEVLTRSSLEVELAAK 306
Cdd:COG5022 1083 LYQLESTENLLKTIN--VKDLEVTNRNLVKPANVLQFIVAQMIKLNL------LQEISKFLSQLVNTLEPVFQKLSVLQL 1154
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 31652236 307 EREIAQLVEDVQRLQAS--LTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYE 363
Cdd:COG5022 1155 ELDGLFWEANLEALPSPppFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELIALFSKI 1213
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
117-447 |
1.05e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 117 QRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKEQKLQNDFAEKERKLQETQMS 196
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLV--QTALRQQEKIERYQADLEELEERLEEQNEV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 197 T---TSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERANQ--------------RAEVAQR 259
Cdd:PRK04863 371 VeeaDEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQT-RAIQYQQAVQALERAKQlcglpdltadnaedWLEEFQA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 260 EAETLREQLSSANHSLQLASQIQKApdVEQAIEVLTRSSLEVelaakEREIAQlvedvQRLQASLTKLRE--NSASQISQ 337
Cdd:PRK04863 450 KEQEATEELLSLEQKLSVAQAAHSQ--FEQAYQLVRKIAGEV-----SRSEAW-----DVARELLRRLREqrHLAEQLQQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 338 LEQQLSAknstlkqLEEKLKGQADYEEVKKELNilKSMEFAPSEGAGTQDAAKPLEVLLLeknrSLQSENAALRISNSDL 417
Cdd:PRK04863 518 LRMRLSE-------LEQRLRQQQRAERLLAEFC--KRLGKNLDDEDELEQLQEELEARLE----SLSESVSEARERRMAL 584
|
330 340 350
....*....|....*....|....*....|
gi 31652236 418 SGRCAELQVRITEAVATATEQRELIARLEQ 447
Cdd:PRK04863 585 RQQLEQLQARIQRLAARAPAWLAAQDALAR 614
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
60-375 |
1.29e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.34 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 60 LRKQVAPLLKSFQGEIDALSKRSK---EAEAAFLNVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEY 136
Cdd:TIGR00618 554 ERKQRASLKEQMQEIQQSFSILTQcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 137 NKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKErkLQETQMSTTSKLEEAEHKvqslQTALE 216
Cdd:TIGR00618 634 LQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQK--MQSEKEQLTYWKEMLAQC----QTLLR 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 217 KTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAET-LREQ-LSSANHSLQLASQIQKAPDVEQAIEVL 294
Cdd:TIGR00618 708 ELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTvLKARtEAHFNNNEEVTAALQTGAELSHLAAEI 787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 295 T-----RSSLEVELAAKEREIAQLVED------------VQRLQASLTKLRENSASQIsQLEQQLSAKNSTLKQLEEKLK 357
Cdd:TIGR00618 788 QffnrlREEDTHLLKTLEAEIGQEIPSdedilnlqcetlVQEEEQFLSRLEEKSATLG-EITHQLLKYEECSKQLAQLTQ 866
|
330
....*....|....*...
gi 31652236 358 GQADYEEVKKELNILKSM 375
Cdd:TIGR00618 867 EQAKIIQLSDKLNGINQI 884
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
56-358 |
1.32e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 56 TPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDpvpaldlgQQLQLKVQRLHDIETENQKLRETLEE 135
Cdd:pfam12128 615 SAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD--------EKQSEKDKKNKALAERKDSANERLNS 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 136 YNKEfaevknqevtIKALKEKIREYEQTLKNQAETIALEKEQKLQNdfAEKERKLQETQMSTTSKLEEAEHKVQslQTAL 215
Cdd:pfam12128 687 LEAQ----------LKQLDKKHQAWLEEQKEQKREARTEKQAYWQV--VEGALDAQLALLKAAIAARRSGAKAE--LKAL 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 216 EKTRTElfDLKTK-YDEETTAK-ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQlasqIQKApDVEQAIEv 293
Cdd:pfam12128 753 ETWYKR--DLASLgVDPDVIAKlKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLA----TQLS-NIERAIS- 824
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31652236 294 ltrsslevelaakereiaqlvedvqRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKG 358
Cdd:pfam12128 825 -------------------------ELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRG 864
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
16-372 |
1.33e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEidALSKRSKEAEaaflNVYKR 95
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE--ELEKKAEEYE----KLKEK 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 96 LIDVPdpvpaldlGQQLQLK--VQRLHDIETENQKLRETLEEYNKEFAEVKNQEV-----TIKALKEKIREYEQtlknqa 168
Cdd:PRK03918 534 LIKLK--------GEIKSLKkeLEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELEP------ 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 169 etiALEKEQKLQNDFAEKERKLQEtQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLE 248
Cdd:PRK03918 600 ---FYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE---EYLELS 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 249 RANQRAEVAQREAETLREQLSSAnhslqlasqiqkAPDVEQAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQAsltKL 327
Cdd:PRK03918 673 RELAGLRAELEELEKRREEIKKT------------LEKLKEELEEREKAKKELEKLEKALErVEELREKVKKYKA---LL 737
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 31652236 328 RENSASQISQLEQQLSAK-------NSTLKQLEEKLKGQADYEEVKKELNIL 372
Cdd:PRK03918 738 KERALSKVGEIASEIFEEltegkysGVRVKAEENKVKLFVVYQGKERPLTFL 789
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
115-455 |
2.09e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.73 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 115 KVQRLHDIETENQKLRETLEEYNKEFaevKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQ 194
Cdd:pfam17380 235 KMERRKESFNLAEDVTTMTPEYTVRY---NGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKARE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 195 MSTTSKLEEAEHKVQSL------------QTALEKTRT-ELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA 261
Cdd:pfam17380 312 VERRRKLEEAEKARQAEmdrqaaiyaeqeRMAMERERElERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 262 ETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEvelAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQ 341
Cdd:pfam17380 392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE---EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 342 LSAKNSTLKQLEEKLKGQADYEEVKKELnILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSGRC 421
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKI-LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQE 547
|
330 340 350
....*....|....*....|....*....|....
gi 31652236 422 AELQVRITEAVATATEQRELIARLEQDLSIIQSI 455
Cdd:pfam17380 548 MEERRRIQEQMRKATEERSRLEAMEREREMMRQI 581
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
196-391 |
2.14e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 196 STTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL 275
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 276 Q-------------LASQIQKAPDVEQAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQ 340
Cdd:COG3883 96 YrsggsvsyldvllGSESFSDFLDRLSALSKIADADADLleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 31652236 341 QLSAKNSTLKQLEEKlkgQADYEEVKKELNILKSMEFAPSEGAGTQDAAKP 391
Cdd:COG3883 176 QQAEQEALLAQLSAE---EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
126-441 |
2.82e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.36 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 126 NQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQA-ETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 204
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 205 EHK-VQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLE--RANQRAE--VAQREAETLREQLSSANHSLQ--- 276
Cdd:pfam07111 138 SQReLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkRAGEAKQlaEAQKEAELLRKQLSKTQEELEaqv 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 277 -LASQIQKAPDvEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAS--LTKLRENSASQISQL-EQQLSAKNSTLKQL 352
Cdd:pfam07111 218 tLVESLRKYVG-EQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATveLLQVRVQSLTHMLALqEEELTRKIQPSDSL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 353 EEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSGRCAELQVritEAV 432
Cdd:pfam07111 297 EPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEV---ERM 373
|
....*....
gi 31652236 433 ATATEQREL 441
Cdd:pfam07111 374 SAKGLQMEL 382
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
21-368 |
3.63e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 21 QRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDlRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVP 100
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED-KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA 1443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 101 DPVPALDLGQQLQLKVQRLHDIETENQKLRETLE--EYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQK 178
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 179 LQN-DFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMImtDLERANQRAEVA 257
Cdd:PTZ00121 1524 ADEaKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA--EEARIEEVMKLY 1601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 258 QREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSslEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQ 337
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK--EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
|
330 340 350
....*....|....*....|....*....|.
gi 31652236 338 LEQQLSAKNSTLKQLEEKLKGQADYEEVKKE 368
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
117-319 |
3.64e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 117 QRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQklqndfAEKERKLQETQmS 196
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREI------AELEAELERLD-A 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 197 TTSKLEEAEHKVQSLQTALEKTRTELFDLKTKY---DEETTAKADEIEMIMTDLERANQRAEVAQRE-AETLREQLSSAN 272
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDA 762
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 31652236 273 HSLQLASQIQKApdveqaievltRSSLEVELAAKEREIAQLVEDVQR 319
Cdd:COG4913 763 VERELRENLEER-----------IDALRARLNRAEEELERAMRAFNR 798
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
25-360 |
3.70e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 25 DATATVLANRQDE----SEQSRKRLIEQ--SREFKKNTPEDLRKQVAPLlksfQGEIDALSKRSKEAEAAFLNVYKRLID 98
Cdd:PRK02224 306 DADAEAVEARREEledrDEELRDRLEECrvAAQAHNEEAESLREDADDL----EERAEELREEAAELESELEEAREAVED 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 99 VPDPVPALDlgQQLQLKVQRLHDIETEnqklRETLEEYNKEFAEVKNqevtikALKEKIREYEQTLKNQAETIALEKEQK 178
Cdd:PRK02224 382 RREEIEELE--EEIEELRERFGDAPVD----LGNAEDFLEELREERD------ELREREAELEATLRTARERVEEAEALL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 179 LQNDFAEKERKLQETQMSTTskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAK--ADEIEMIMTDLERANQRAEV 256
Cdd:PRK02224 450 EAGKCPECGQPVEGSPHVET--IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaEDRIERLEERREDLEELIAE 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 257 AQREAETLREQLSSANHSLQ-LASQIQKAPDVEQAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQ--ASLTKLRENSAS 333
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAeLEAEAEEKREAAAEAEEEAEEARE-EVAELNSKLAELKERIESLEriRTLLAAIADAED 606
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 31652236 334 QISQLEQQ--------------LSAKNSTLKQLEEKLKGQA 360
Cdd:PRK02224 607 EIERLREKrealaelnderrerLAEKRERKRELEAEFDEAR 647
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
14-268 |
3.84e-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: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 14 RFDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTP-----EDLRKQVAPLLKSFQGEIDALSKRSKEAEAA 88
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaeaEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 89 FLNVYKRlidvpdpvpALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQA 168
Cdd:TIGR02168 812 LTLLNEE---------AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNER 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 169 ETI--ALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTD 246
Cdd:TIGR02168 883 ASLeeALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY---SLTLEEAEAL 959
|
250 260
....*....|....*....|..
gi 31652236 247 LERANQRAEVAQREAETLREQL 268
Cdd:TIGR02168 960 ENKIEDDEEEARRRLKRLENKI 981
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
117-283 |
3.95e-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: 43.86 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 117 QRLHDIETENQKLRETLEEYNKEFAEvKNQEvtIKALKEKIREYEQTLKNQAETIA--LEKEQKLQNDFAEKERKLQETQ 194
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKS-KEKE--LKKLNEEKKELEEKVKDLTKKISslKEKIEKLESEKKEKESKISDLE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 195 -----MSTTSKLEEAEHKVQSLQ----------TALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQR 259
Cdd:TIGR04523 545 delnkDDFELKKENLEKEIDEKNkeieelkqtqKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
170 180
....*....|....*....|....*...
gi 31652236 260 EAETLREQ----LSSANHSLQLASQIQK 283
Cdd:TIGR04523 625 ENEKLSSIikniKSKKNKLKQEVKQIKE 652
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
18-216 |
4.13e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 18 QQLQRELDATATVLANRQDESEQSRKRLIEQS---REFKKNT----PEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFL 90
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEaalEEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 91 NVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAET 170
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEA 320
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 31652236 171 ---IALEKEQKLQNDFAEKERKLQETQmSTTSKLEEAEHKVQSLQTALE 216
Cdd:COG3206 321 eleALQAREASLQAQLAQLEARLAELP-ELEAELRRLEREVEVARELYE 368
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
58-250 |
5.32e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.74 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 58 EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLNVYKRLIDvpdpvpalDLGQQLQLKVQRLHDI-ETENQKL-RETLEE 135
Cdd:cd22656 113 EEAKKTIKALLDDLLKEAKKYQDKAAKVVDK-LTDFENQTE--------KDQTALETLEKALKDLlTDEGGAIaRKEIKD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 136 YNKEFAevKNQEVTIKALKEKIREYEQTLKNQAETIAleKEQKLQNDFaekerKLQETQM-STTSKLEEAEHKVQSLQTA 214
Cdd:cd22656 184 LQKELE--KLNEEYAAKLKAKIDELKALIADDEAKLA--AALRLIADL-----TAADTDLdNLLALIGPAIPALEKLQGA 254
|
170 180 190
....*....|....*....|....*....|....*.
gi 31652236 215 LEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERA 250
Cdd:cd22656 255 WQAIATDLDSLKDLLEDDIS-KIPAAILAKLELEKA 289
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
250-497 |
5.36e-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: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 250 ANQRAEVAQREAETLREQLSSANHslQLASQIQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRE 329
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEK--ELAALKKEEKALLKQLA-----ALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 330 nsasQISQLEQQLSAKNSTLKQLEEKL--KGQADYEEVkkelnILKSMEFAPSE------GAGTQDAAKPLEVLLLEKNR 401
Cdd:COG4942 91 ----EIAELRAELEAQKEELAELLRALyrLGRQPPLAL-----LLSPEDFLDAVrrlqylKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 402 sLQSENAALRISNSDLSGRCAELQVRITEAVATATEQRELIARLEQDLSIIQsiQRPDAEGAAEHRLEKIPEPIKEATAL 481
Cdd:COG4942 162 -LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA--AELAELQQEAEELEALIARLEAEAAA 238
|
250
....*....|....*.
gi 31652236 482 FYGPAAPASGALPEGQ 497
Cdd:COG4942 239 AAERTPAAGFAALKGK 254
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
21-246 |
5.37e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 21 QRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaaflnvykrlidvP 100
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE-------------E 1658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 101 DPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKnqAETIALEKEQKLQ 180
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAEEAK 1736
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31652236 181 NDFAEKERKLQETQmsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD 246
Cdd:PTZ00121 1737 KEAEEDKKKAEEAK-----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
117-250 |
6.97e-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: 41.83 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 117 QRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQTL---KNQAETIALEKEQklqnDFAEKERK 189
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELedleKEIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQKEI----ESLKRRIS 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31652236 190 LQETQMS-TTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERA 250
Cdd:COG1579 107 DLEDEILeLMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
174-556 |
8.78e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.42 E-value: 8.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 174 EKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRtELFDLKTKYDEETTAKADEIEMIMTDLERANQR 253
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN-EKESQLADAREVISCLKNELSELRRQIQRAELE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 254 AEVAQREAETLREQL----------SSANHSLQ-----LASQIQKAPDVEQAIEVLTRSSLEVELAAKERE-IAQLVEDV 317
Cdd:pfam05557 127 LQSTNSELEELQERLdllkakaseaEQLRQNLEkqqssLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELArIPELEKEL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 318 QRLQASLTKLRENSASqISQLEQQLSAKNSTLKQLE----EKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPL- 392
Cdd:pfam05557 207 ERLREHNKHLNENIEN-KLLLKEEVEDLKRKLEREEkyreEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRi 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 393 ------EVLLLEKNRSLQSENAALRISNSDLSGRCAELQVRITEAVATATEQRELIARLEQDLSII--------QSIQRP 458
Cdd:pfam05557 286 eqlqqrEIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLtkerdgyrAILESY 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 459 DAEGAAEHRLEKIPEPIKEATALFYGPAAPASGAlpEGQVDSLLSIISSQRERFRA--------RNQELEAENRLAQHTL 530
Cdd:pfam05557 366 DKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEM--EAQLSVAEEELGGYKQQAQTlerelqalRQQESLADPSYSKEEV 443
|
410 420
....*....|....*....|....*.
gi 31652236 531 QALQSELDSLRADNIKLFEKIKFLQS 556
Cdd:pfam05557 444 DSLRRKLETLELERQRLREQKNELEM 469
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
66-371 |
1.05e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.59 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 66 PLLKSFQGEIDALSKRsKEAEAAFLNVYKRLIDvpdpvpALDLGQQLQlkvqrlhDIETENQKLRETLEEYNKEFAEVKN 145
Cdd:PRK11281 36 PTEADVQAQLDALNKQ-KLLEAEDKLVQQDLEQ------TLALLDKID-------RQKEETEQLKQQLAQAPAKLRQAQA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 146 QevtIKALKEKIreyEQTLKNQAETIALEKeqkLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKTRTELFdl 225
Cdd:PRK11281 102 E---LEALKDDN---DEETRETLSTLSLRQ---LESRLAQTLDQLQNAQ----NDLAEYNSQLVSLQTQPERAQAALY-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 226 ktkydeettakadeiemimtdlerANQraevaQREAEtLREQLSSANHSlqlasqiQKAPDVEQaievltRSSLEVELAA 305
Cdd:PRK11281 167 ------------------------ANS-----QRLQQ-IRNLLKGGKVG-------GKALRPSQ------RVLLQAEQAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 306 KEREIA---QLVEDVQRLQASLTKLRENSASQISQLEQQL-------SAKNSTLKQ--------LEEKLKGQADyEEVKK 367
Cdd:PRK11281 204 LNAQNDlqrKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLqllqeaiNSKRLTLSEktvqeaqsQDEAARIQAN-PLVAQ 282
|
....
gi 31652236 368 ELNI 371
Cdd:PRK11281 283 ELEI 286
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
16-359 |
1.17e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 16 DLQQLQRELDATATVLANRQDESEQSRKRL------------IEQSREFKKNTPEDLRKQVApLLKSFQGEIDALSKRSK 83
Cdd:PRK04863 308 RLVEMARELAELNEAESDLEQDYQAASDHLnlvqtalrqqekIERYQADLEELEERLEEQNE-VVEEADEQQEENEARAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 84 EAEAAFLNVYKRLIDVpdpVPALDLGQ----QLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtiKALKEKIRE 159
Cdd:PRK04863 387 AAEEEVDELKSQLADY---QQALDVQQtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE---QEATEELLS 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 160 YEQTLkNQAETIALEKEQKLQ---NDFAEKERK-LQETQMSTTSKLEEAEHKVQSLQTAlektRTELFDLKTKYDEETTA 235
Cdd:PRK04863 461 LEQKL-SVAQAAHSQFEQAYQlvrKIAGEVSRSeAWDVARELLRRLREQRHLAEQLQQL----RMRLSELEQRLRQQQRA 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 236 kadeiEMIMTDLERANQRAEVAQREAETLREQLSSA--NHSLQLASQIQKAPDVEQAIEvltrsslevELAAKEREIAQL 313
Cdd:PRK04863 536 -----ERLLAEFCKRLGKNLDDEDELEQLQEELEARleSLSESVSEARERRMALRQQLE---------QLQARIQRLAAR 601
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 31652236 314 VEDVQRLQASLTKLRENS------ASQISQLEQQLSAKNSTLKQLEEKLKGQ 359
Cdd:PRK04863 602 APAWLAAQDALARLREQSgeefedSQDVTEYMQQLLERERELTVERDELAAR 653
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
14-541 |
1.56e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 14 RFDLQQLQRELDATATV----LANRQDESEQSRKRLIEQSR----------EFKKNTPEDLRKQVAPLLKSFQGEIDALS 79
Cdd:pfam15921 144 RNQLQNTVHELEAAKCLkedmLEDSNTQIEQLRKMMLSHEGvlqeirsilvDFEEASGKKIYEHDSMSTMHFRSLGSAIS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 80 KRSKEAEAAFLNVYKRLIDVPDPVPALDlgQQLQLKVQRLhdIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIRE 159
Cdd:pfam15921 224 KILRELDTEISYLKGRIFPVEDQLEALK--SESQNKIELL--LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 160 YEQTLKNQAE---TIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTElfdlKTKYDEETTAK 236
Cdd:pfam15921 300 QLEIIQEQARnqnSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTE----RDQFSQESGNL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 237 ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-QLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVE 315
Cdd:pfam15921 376 DDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIdHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQG 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 316 DVQRLQ--ASLTKLRENSASQISQLEQQLSAKNSTLKQ-----------LEEKLKG----QADYEEVKKELNI-LKSMEF 377
Cdd:pfam15921 456 KNESLEkvSSLTAQLESTKEMLRKVVEELTAKKMTLESsertvsdltasLQEKERAieatNAEITKLRSRVDLkLQELQH 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 378 APSEGAGTQDAAKPLEVLLL---EKNRSL-----QSEN------------AALRISNSDLSGRCAELQVRITEAVATATE 437
Cdd:pfam15921 536 LKNEGDHLRNVQTECEALKLqmaEKDKVIeilrqQIENmtqlvgqhgrtaGAMQVEKAQLEKEINDRRLELQEFKILKDK 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 438 QRELIARLEQDLSIIQsIQRPDAEGAAEHRLEKIPEPIKEATALFYGPAAPASgalpegQVDSLLSIISSQRERFRARNQ 517
Cdd:pfam15921 616 KDAKIRELEARVSDLE-LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRN------ELNSLSEDYEVLKRNFRNKSE 688
|
570 580
....*....|....*....|....
gi 31652236 518 ELEAENRLAQHTLQALQSELDSLR 541
Cdd:pfam15921 689 EMETTTNKLKMQLKSAQSELEQTR 712
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
118-227 |
1.61e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 118 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAET---IALEKEQKLQNDFA---EKERKLQ 191
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELDrakEKLKKLL 217
|
90 100 110
....*....|....*....|....*....|....*.
gi 31652236 192 ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKT 227
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT 253
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
119-416 |
1.70e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.96 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 119 LHDIETENQKLRETLEEYNKEFAevKNQEVTI--------KALKEKIREYEQTLKNqAETIALEKEQKLQNDFAEKERKL 190
Cdd:TIGR01612 988 LNDYEAKNNELIKYFNDLKANLG--KNKENMLyhqfdekeKATNDIEQKIEDANKN-IPNIEIAIHTSIYNIIDEIEKEI 1064
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 191 -QETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKydEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQls 269
Cdd:TIGR01612 1065 gKNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGK--EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKK-- 1140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 270 SANHSLQLASQIQKAPDVeqAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLEQQLSA----K 345
Cdd:TIGR01612 1141 SENYIDEIKAQINDLEDV--ADKAISNDDPE-EIEKKIENIVTKIDKKKNIYDEIKKL----LNEIAEIEKDKTSleevK 1213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31652236 346 NSTL---KQLEEKLKGQADyEEVKKELNILKSMEfAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSD 416
Cdd:TIGR01612 1214 GINLsygKNLGKLFLEKID-EEKKKSEHMIKAME-AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDD 1285
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
151-448 |
1.87e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 151 KALKEKIREYEQTLKNQAETIALEK-EQKLQNDFAEKERKLQETQmsttsKLEEAEhkvqsLQTALEKTRTELFDLKTKY 229
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLqELKLKEQAKKALEYYQLKE-----KLELEE-----EYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 230 DEETTAKADEIEMImtdleraNQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKERE 309
Cdd:pfam02463 243 QELLRDEQEEIESS-------KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 310 IAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSmefapSEGAGTQDAA 389
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK-----LESERLSSAA 390
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 31652236 390 KPLEVLLLEKNRSLQSENAALRISNSDLSGRCAELQVRITEAVATATEQRELIARLEQD 448
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEE 449
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
127-450 |
2.13e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 127 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYE----------QTLKNQAETIALEKE-------------------- 176
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAETErereelaeevRDLRERLEELEEERDdllaeaglddadaeavearr 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 177 QKLQNDFAEKERKLQETQMSTTSKLEEAE-----------------HKVQSLQTALEKTRTELFDLKTK---YDEETTAK 236
Cdd:PRK02224 317 EELEDRDEELRDRLEECRVAAQAHNEEAEslredaddleeraeelrEEAAELESELEEAREAVEDRREEieeLEEEIEEL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 237 ADEIEMIMTDLERANQRAEVAQREAETLREQ-------LSSANHSLQLASQIQ---KAPDVEQAIE----VLTRSSLEVE 302
Cdd:PRK02224 397 RERFGDAPVDLGNAEDFLEELREERDELREReaeleatLRTARERVEEAEALLeagKCPECGQPVEgsphVETIEEDRER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 303 LAAKEREIAQLVEDVQRLQASLTKLRE--NSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKElnilkSMEFAPS 380
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERLERAEDlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE-----RAAELEA 551
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 381 EGAGTQDAAKPLEvllleknrslqSENAALRISNSDLSGRCAELQVRItEAVATATEQRELIARLEQDLS 450
Cdd:PRK02224 552 EAEEKREAAAEAE-----------EEAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIE 609
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
18-461 |
3.11e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 18 QQLQRELDATATVLANRQDESEQSRKRLIEQSREFK-KNTPEDLRKQVApllksfQGEIDALSKRSKEAEAAfLNVYKRL 96
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEeKKKADEAKKAEE------KKKADEAKKKAEEAKKA-DEAKKKA 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 97 IDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKA--LKEKIREYEQT---------LK 165
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAdaAKKKAEEKKKAdeakkkaeeDK 1404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 166 NQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTElfDLKTKYDEETtaKADEIEMIMT 245
Cdd:PTZ00121 1405 KKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAE--EAKKKAEEAK--KADEAKKKAE 1480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 246 DLERANQ---RAEVAQREAETLREQLSSANHSLQL--------------------ASQIQKAPDVEQAIEVltRSSLEVE 302
Cdd:PTZ00121 1481 EAKKADEakkKAEEAKKKADEAKKAAEAKKKADEAkkaeeakkadeakkaeeakkADEAKKAEEKKKADEL--KKAEELK 1558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 303 LAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQAD----YEEVKKELNILKSMEfa 378
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikAEELKKAEEEKKKVE-- 1636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 379 psegagtqdAAKPLEVLLLEKNRSLQSENAALRISNSDLSGRCAELQVRITEAVATATEQR---ELIARLEQDLSIIQSI 455
Cdd:PTZ00121 1637 ---------QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKkaaEALKKEAEEAKKAEEL 1707
|
....*.
gi 31652236 456 QRPDAE 461
Cdd:PTZ00121 1708 KKKEAE 1713
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
110-555 |
3.38e-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: 40.87 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 110 QQLQLKVQRLHDIETENQKLRETLEeynKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQN------DF 183
Cdd:pfam15921 120 QEMQMERDAMADIRRRESQSQEDLR---NQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEirsilvDF 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 184 AEKERK--LQETQMSTT--SKLEEAEHKV-QSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD-LERANQRAEVA 257
Cdd:pfam15921 197 EEASGKkiYEHDSMSTMhfRSLGSAISKIlRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQhQDRIEQLISEH 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 258 QREAETLREQLSSANhslqlasqiQKAPDVEQAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQ 337
Cdd:pfam15921 277 EVEITGLTEKASSAR---------SQANSIQSQLEIIQEQARN-QNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 338 LEQQLSAKNSTLKQ--------------LEEKL-KGQADYEEVKKELNILKSM-EFAPSEGAGTQDAAKPLEVLLLEKNR 401
Cdd:pfam15921 347 LEKQLVLANSELTEarterdqfsqesgnLDDQLqKLLADLHKREKELSLEKEQnKRLWDRDTGNSITIDHLRRELDDRNM 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 402 SLQSENAALRISNSDLSGRCAelqvRITEAVATATEQRELIARLEQDLSIIQSIQRPDAE--GAAEHRLEKIPEPIKEAT 479
Cdd:pfam15921 427 EVQRLEALLKAMKSECQGQME----RQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEelTAKKMTLESSERTVSDLT 502
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31652236 480 alfygpaapASGALPEGQVDSLLSIISSQRERFRARNQELEAENRLAQHtLQALQSELDSLRadnIKLFEKIKFLQ 555
Cdd:pfam15921 503 ---------ASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDH-LRNVQTECEALK---LQMAEKDKVIE 565
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
122-327 |
3.43e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 122 IETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYeqtlKNQAETIALEKEQKLqndFAEKERKLQETQMSTTSKL 201
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKE---LEEAEAALEEF----RQKNGLVDLSEEAKL---LLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 202 EEAEHKVQSLQTALEKT----------------RTELFDLKTKYDEE-TTAKADEIEMIMTDLERANQRAEVAQREAETL 264
Cdd:COG3206 236 AEAEARLAALRAQLGSGpdalpellqspviqqlRAQLAELEAELAELsARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31652236 265 REQLSsanhslQLASQIQKAPDVEQAIEVLTRSSLEveLAAKEREIAQLVEDVQRLQASLTKL 327
Cdd:COG3206 316 ASLEA------ELEALQAREASLQAQLAQLEARLAE--LPELEAELRRLEREVEVARELYESL 370
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
109-354 |
3.46e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 109 GQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIalekeQKLQNDFAEKER 188
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI-----RELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 189 KLQ--ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLRE 266
Cdd:PRK03918 274 EIEelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE-KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 267 QLSSANHSLQLasqiqkapdVEQAIEVLTR-SSLEVELAAKERE-IAQLVEDVQRLQASLTKLRENSASQISQLEQQLSA 344
Cdd:PRK03918 353 RLEELEERHEL---------YEEAKAKKEElERLKKRLTGLTPEkLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250
....*....|
gi 31652236 345 KNSTLKQLEE 354
Cdd:PRK03918 424 LKKAIEELKK 433
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
130-410 |
3.86e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 130 RETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETialekEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQ 209
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR-----KKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 210 SLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQ---------REAETLREQLSSANHSLQLASQ 280
Cdd:TIGR00606 312 RTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQehirardslIQSLATRLELDGFERGPFSERQ 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 281 IQKAPDVE---QAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLK 357
Cdd:TIGR00606 392 IKNFHTLVierQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD 471
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 31652236 358 G--QADYEEVKKELNILKSMEFAPSEGAGTQDAA-KPLEVLLLEKNRSLQSENAAL 410
Cdd:TIGR00606 472 RilELDQELRKAERELSKAEKNSLTETLKKEVKSlQNEKADLDRKLRKLDQEMEQL 527
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
119-378 |
4.14e-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: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 119 LHDIETENQKLRETL----EEYNKEFAEVKNQEVTIKALKEKIREYEQTL-KNQAETIALE-KEQKLQNDFAEKERKLQE 192
Cdd:pfam10174 249 IRDLEDEVQMLKTNGllhtEDREEEIKQMEVYKSHSKFMKNKIDQLKQELsKKESELLALQtKLETLTNQNSDCKQHIEV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 193 TQMSTTSKLEEA---EHKVQSLQTALEKTRTeLFDLKTKY----DEETTAKADEIEMIMTDLERANQRAEVAQREAETLR 265
Cdd:pfam10174 329 LKESLTAKEQRAailQTEVDALRLRLEEKES-FLNKKTKQlqdlTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQ 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 266 EQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQ-------ASLTKLRENSASQISQL 338
Cdd:pfam10174 408 EQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDrerleelESLKKENKDLKEKVSAL 487
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 31652236 339 EQQLSAKNSTLKQLEEKLKGQAdyEEVKKELNILKSMEFA 378
Cdd:pfam10174 488 QPELTEKESSLIDLKEHASSLA--SSGLKKDSKLKSLEIA 525
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
299-580 |
4.85e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 299 LEVELAAKEREIAQLVEDVQRLQAsltklrensasQISQLEQQLSAknstLKQLEEKLKGQADYEEVKKELnilksmefa 378
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEA-----------ELDALQERREA----LQRLAEYSWDEIDVASAEREI--------- 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 379 psegagtqdaakplevllleknRSLQSENAALRISNSDLsgrcAELQVRITEAVATATEQRELIARLEQDlsiiqsiqrp 458
Cdd:COG4913 671 ----------------------AELEAELERLDASSDDL----AALEEQLEELEAELEELEEELDELKGE---------- 714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 459 daEGAAEHRLEKIPEPIKEATALFYGPAAPASGALpegqvdsllsiissqRERFRARNQELEAENRLAQHtLQALQSELD 538
Cdd:COG4913 715 --IGRLEKELEQAEEELDELQDRLEAAEDLARLEL---------------RALLEERFAAALGDAVEREL-RENLEERID 776
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 31652236 539 SLRADNIKLFEKI-----KFLQSYPGRGSGSdDTELRYSSQYEERLD 580
Cdd:COG4913 777 ALRARLNRAEEELeramrAFNREWPAETADL-DADLESLPEYLALLD 822
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
113-268 |
5.69e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.12 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 113 QLKVQRLhDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKEQKLQNDFAEKERKLQE 192
Cdd:COG1340 75 ELKEERD-ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ--QTEVLSPEEEKELVEKIKELEKELEK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 193 TQMS--TTSKLEEAEHKVQSLQTALEKTR---TELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQ 267
Cdd:COG1340 152 AKKAleKNEKLKELRAELKELRKEAEEIHkkiKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEE 231
|
.
gi 31652236 268 L 268
Cdd:COG1340 232 I 232
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
250-546 |
5.69e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 250 ANQRAEVAQREAETLREQLSSANhSLQLASQIQKA--PDVEQAIEVLTR--------SSLEVELAAKEREIAQLVEDVQR 319
Cdd:PRK11281 27 ARAASNGDLPTEADVQAQLDALN-KQKLLEAEDKLvqQDLEQTLALLDKidrqkeetEQLKQQLAQAPAKLRQAQAELEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 320 LQASLTK-LRENSASQ-ISQLEQQLSAKNSTLKQLEEKLkgqADY-----------EEVKKEL--NILKSMEFApSEGAG 384
Cdd:PRK11281 106 LKDDNDEeTRETLSTLsLRQLESRLAQTLDQLQNAQNDL---AEYnsqlvslqtqpERAQAALyaNSQRLQQIR-NLLKG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 385 TQDAAKPLEVLLLEKnrsLQSENAALRISNSDlsgRCAELQVrITEAVATATEQREL----IARLEQDLSIIQSIqrpda 460
Cdd:PRK11281 182 GKVGGKALRPSQRVL---LQAEQALLNAQNDL---QRKSLEG-NTQLQDLLQKQRDYltarIQRLEHQLQLLQEA----- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 461 egAAEHRLEKIPEPIKEATalfygpaapASGALPEGQVDSLLSiissqrerfrarnQELEAENRLAQHTLQALQsELDSL 540
Cdd:PRK11281 250 --INSKRLTLSEKTVQEAQ---------SQDEAARIQANPLVA-------------QELEINLQLSQRLLKATE-KLNTL 304
|
....*.
gi 31652236 541 RADNIK 546
Cdd:PRK11281 305 TQQNLR 310
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
122-360 |
5.83e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.21 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 122 IETENQKLRETLEEYNKEFAEVKNQevtikaLKEKIREYEQTLKNQAETIALEKEQ---------KLQNDFAEKERKLQE 192
Cdd:pfam12128 274 IASRQEERQETSAELNQLLRTLDDQ------WKEKRDELNGELSAADAAVAKDRSElealedqhgAFLDADIETAAADQE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 193 TQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDLE-----RANQRAE---VAQREAETL 264
Cdd:pfam12128 348 QLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN---NRDIAGIKDKLAkireaRDRQLAVaedDLQALESEL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 265 REQLSSANHSL------------QLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQL-VEDVQRLQASLTKLRENS 331
Cdd:pfam12128 425 REQLEAGKLEFneeeyrlksrlgELKLRLNQATATPELLLQLENFDERIERAREEQEAANAeVERLQSELRQARKRRDQA 504
|
250 260
....*....|....*....|....*....
gi 31652236 332 ASQISQLEQQLSAKNSTLKQLEEKLKGQA 360
Cdd:pfam12128 505 SEALRQASRRLEERQSALDELELQLFPQA 533
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
125-222 |
6.08e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 125 ENQKLRETLEEynkefaEVKNQEVTIKALKEKIREYEQTLKNQAEtiALEKeqklqndfaeKERKLQETQMSTTSKLEEA 204
Cdd:PRK12704 65 EIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLE--LLEK----------REEELEKKEKELEQKQQEL 126
|
90
....*....|....*...
gi 31652236 205 EHKVQSLQTALEKTRTEL 222
Cdd:PRK12704 127 EKKEEELEELIEEQLQEL 144
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
172-569 |
6.46e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 39.94 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 172 ALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALektrtelfdlktkydeettAKADEIEMIMTDLERAN 251
Cdd:COG3096 300 QLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTAL-------------------RQQEKIERYQEDLEELT 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 252 QRAEVAQREAETLREQLSSANHSLQLASQ------IQKApDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAslt 325
Cdd:COG3096 361 ERLEEQEEVVEEAAEQLAEAEARLEAAEEevdslkSQLA-DYQQALDVQQTRAIQYQQAVQALEKARALCGLPDLTP--- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 326 klrENSASQISQLEQQLSAKNSTLKQLEEKLK-GQADYEEVKKELNILKSMefapsEGAGTQDAAKPLEVLLLEKNRSLQ 404
Cdd:COG3096 437 ---ENAEDYLAAFRAKEQQATEEVLELEQKLSvADAARRQFEKAYELVCKI-----AGEVERSQAWQTARELLRRYRSQQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 405 SENA---ALRISNSDLSGRCA----------ELQVRITEAVATATEQRELIARLEQDLSIIQSIQRPDAEGAAEHR--LE 469
Cdd:COG3096 509 ALAQrlqQLRAQLAELEQRLRqqqnaerlleEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRqqLE 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 470 KIPEPIKE--ATALFYGPAAPASGALPEGQVDSLLSI--ISSQRERFRARNQELEAENRLAQHTLQALQSELDSLRAdni 545
Cdd:COG3096 589 QLRARIKElaARAPAWLAAQDALERLREQSGEALADSqeVTAAMQQLLEREREATVERDELAARKQALESQIERLSQ--- 665
|
410 420
....*....|....*....|....
gi 31652236 546 klfekikflqsypgrGSGSDDTEL 569
Cdd:COG3096 666 ---------------PGGAEDPRL 674
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
125-370 |
6.60e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.95 E-value: 6.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 125 ENQKLRETLE---EYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKL 201
Cdd:pfam02463 174 ALKKLIEETEnlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 202 EEAEhKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA--ETLREQLSSANHSLQLAS 279
Cdd:pfam02463 254 ESSK-QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDeeKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 280 QIQKAPDVEQAIEVLTRSSLEVELA--AKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLK 357
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEeeELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412
|
250
....*....|...
gi 31652236 358 GQADYEEVKKELN 370
Cdd:pfam02463 413 LARQLEDLLKEEK 425
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
115-267 |
9.22e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 9.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 115 KVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQ 194
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31652236 195 MSTTSKLEEAE-HKVQSLQTALEKTRTELFDLKTKyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQ 267
Cdd:PTZ00121 1704 AEELKKKEAEEkKKAEELKKAEEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
32-277 |
9.30e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 39.35 E-value: 9.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 32 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVpdpvpaldLGQQ 111
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQ--------LSKK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 112 LQ-LKVQRLHDIETENQKLRETLE----------EYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQ 180
Cdd:pfam09731 303 LAeLKKREEKHIERALEKQKEELDklaeelsarlEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLK 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652236 181 NDFAEKERKLQETQMsttskleeaehkvQSLQTALEKTRtelfDLKTKYDEETTAKADEIEMIMT---DLERANQRAEVA 257
Cdd:pfam09731 383 DVLVEQEIELQREFL-------------QDIKEKVEEER----AGRLLKLNELLANLKGLEKATSshsEVEDENRKAQQL 445
|
250 260
....*....|....*....|
gi 31652236 258 QREAETLREQLSSANHSLQL 277
Cdd:pfam09731 446 WLAVEALRSTLEDGSADSRP 465
|
|
| |
