|
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 ... |
421-641 |
5.55e-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: 220.24 E-value: 5.55e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 421 ELQIHLTEATAKAVEQKELIARLEQDLSTIQSIQR--PDAEGASEQGLEKIPEPIKEATAlfyGPSMSSSGTLPEGQV-- 496
Cdd:pfam08172 1 TLQEELSSLNAELEEQQELNAKLENDLLKVQDEASnaFSFNDASSAGSGVSRYPPSGGRR---SPTSSIISGFEPSESss 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 497 ---DSLLSIISSQRERFRTRNQELEAESRMAQHTIQALQSELDSLRADNIKLFEKIKFLQSYPGRGIGSDDTEL------ 567
Cdd:pfam08172 78 ssdSSILPIVTSQRDRFRQRNAELEEELRKQFETISSLRQEIASLQKDNLKLYEKTRYLQSYNRGGGGGTKSSSstsssa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 568 ----------------RYSSQYEERLDPFSSFSKRERQRKYLGLSPWDKATLGMGRLILSNKMARTISFFYTLFLHCLVF 631
Cdd:pfam08172 158 saygnnpnpsdvealdKYRKAYEESLNPFAAFRGRESERAYKRLSPLERLVLSLTRLVLANRTSRNLFFFYCLALHLLVF 237
|
250
....*....|
gi 110815859 632 LVLYKLAWSE 641
Cdd:pfam08172 238 FTLYYVSNSS 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-375 |
4.19e-12 |
|
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: 69.70 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 107 DVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIA--LEKEQKLQNDFA 184
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEerIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 185 EKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQRA 254
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 255 EVAQREAETLREQLSSANHSLqlaSQIQKAPDVAIEVLTrsSLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQIS 334
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEI---EELEELIEELESELE--ALLNERASLEEALALLRSELEELSEELRELES----KRS 911
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 110815859 335 QLEQQLNAKNSTLKQLEEKLKG-QADYEEVKKELNTLKSMEF 375
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGlEVRIDNLQERLSEEYSLTL 953
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
111-362 |
1.34e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 111 QLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREyEQTLKSQAETIALEKEQKLQNDFAEKERKL 190
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL-ELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 191 ---QETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMimtdLERANQRAEVAQREAETLREQ 267
Cdd:COG1196 305 arlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE----LAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 268 LSSANHSLQ--LASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNS 345
Cdd:COG1196 381 LEELAEELLeaLRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250
....*....|....*..
gi 110815859 346 TLKQLEEKLKGQADYEE 362
Cdd:COG1196 461 LLELLAELLEEAALLEA 477
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
123-455 |
2.22e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 123 ETENQ--KLRETLEEYNKEFAEVKNQEVTIKALKEKIREYeQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSK 200
Cdd:TIGR02168 176 ETERKleRTRENLDRLEDILNELERQLKSLERQAEKAERY-KELKAELRELELALLVLRLEELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 201 LEEAEHKLQTLQTALEKTRTELFDLKTKYDEETT---AKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQL 277
Cdd:TIGR02168 255 LEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 278 ASQIQKAPDVAIEVLTRSSleVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQ 357
Cdd:TIGR02168 335 LAEELAELEEKLEELKEEL--ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 358 ADYEEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEknrsLQSENATLRISNSDLSGRCAELQIHLTEATAKAVEQK 437
Cdd:TIGR02168 413 EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE----LQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
330
....*....|....*...
gi 110815859 438 ELIARLEQDLSTIQSIQR 455
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSE 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-367 |
3.18e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 18 QQLQRELDATATVLANRQDESEQSRKRLIEQsrefkkntpedlrkqvapllksfqgEIDALSKRSKEAEAAFltvykrli 97
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEA-------------------------ELEELEAELEELEAEL-------- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 98 dvpdpvpaldvgQQLEIKVQRLHD-IETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKE 176
Cdd:COG1196 263 ------------AELEAELEELRLeLEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 177 QklQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKtkyDEETTAKADEIEMIMTDLERANQRAEV 256
Cdd:COG1196 331 E--LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE---EELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 257 AQREAETLREQLSSANHSLQLASQIQKApdvAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQL 336
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAEL---EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
330 340 350
....*....|....*....|....*....|.
gi 110815859 337 EQQLNAKNSTLKQLEEKLKGQADYEEVKKEL 367
Cdd:COG1196 483 LEELAEAAARLLLLLEAEADYEGFLEGVKAA 513
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-452 |
1.07e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 112 LEIKVQRLHDIETEnqklRETLEEYnkefaevknqevtiKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQ 191
Cdd:TIGR02169 193 IDEKRQQLERLRRE----REKAERY--------------QALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 192 ETQMSTTSKLEEAEHKLQTLQTALEKtrtelfdLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsa 271
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKK-------IKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA-- 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 272 nhslQLASQIQKApdvaieVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRensaSQISQLEQQLNAKNSTLKQLE 351
Cdd:TIGR02169 326 ----KLEAEIDKL------LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR----AELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 352 EKLkgqadyEEVKKELNTLKsmefapsegaGTQDStkplevlLLEKNRSLQSENATLRISNSDLSGRCAELQIHLTEATA 431
Cdd:TIGR02169 392 EKL------EKLKREINELK----------RELDR-------LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
330 340
....*....|....*....|.
gi 110815859 432 KAVEQKELIARLEQDLSTIQS 452
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYEQ 469
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
13-541 |
2.48e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 13 KRFDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNtpedlRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTV 92
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER-----LEELEEELAELEEELEELEEELEELEEELEEA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 93 YKRLidvpdpvpaLDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIA 172
Cdd:COG1196 350 EEEL---------EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 173 LEKEQKLQNDFAEKERKLQETQmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEmimtDLERANQ 252
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEE-----ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE----ELAEAAA 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 253 RAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKE--REIAQLVEDVQRLQASLTKLRENSA 330
Cdd:COG1196 492 RLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALaaALQNIVVEDDEVAAAAIEYLKAAKA 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 331 SQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEFAPSE-------GAGTQDSTKPLEVLLLEKNRSLQS 403
Cdd:COG1196 572 GRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDtllgrtlVAARLEAALRRAVTLAGRLREVTL 651
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 404 ENATLRISNSDLSGRCAELQIHLTEATAKAVEQKELIARLEQDLSTIQSIQRPDAEGASEQGLEKIPEPIKEATAlfygp 483
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL----- 726
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 110815859 484 smsssgtlpEGQVDSLLSIISSQRERFRTRNQELEAESRMAQHTIQALQSELDSLRAD 541
Cdd:COG1196 727 ---------EEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-332 |
2.60e-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: 56.31 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 105 ALDVGQQLEIKVQRLH-DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIAL--EKEQKLQN 181
Cdd:COG4942 18 QADAAAEAEAELEQLQqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEleKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 182 DFAEKERKLQET--QMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEEttaKADEIEMIMTDLERANQRAEVAQR 259
Cdd:COG4942 98 ELEAQKEELAELlrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE---QAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110815859 260 EAETLREQLSSANHSLQLASQIQKApdvaievlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 332
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQK--------LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
67-372 |
5.24e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 5.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 67 LLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPALDvgQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVknq 146
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLE--QEEEKLKERLEELEEDLSSLEQEIENVKSELKEL--- 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 147 EVTIKALKEKIREYEQTLKSQAETIALEKEQKLQN--DFAEKERKLQETQmstTSKLEEAEHKLQTLQTALEKTRTELFD 224
Cdd:TIGR02169 764 EARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAelSKLEEEVSRIEAR---LREIEQKLNRLTLEKEYLEKEIQELQE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 225 LKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS-----ANHSLQLASQIQKAPDVAIEVLTRSSLEV 299
Cdd:TIGR02169 841 QRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDlkkerDELEAQLRELERKIEELEAQIEKKRKRLS 920
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110815859 300 ELAAKEREIAQLVEDVQRLQASLTKLRENSASqISQLEQQLNAKNSTLKQLEE-KLKGQADYEEVKKELNTLKS 372
Cdd:TIGR02169 921 ELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRALEPvNMLAIQEYEEVLKRLDELKE 993
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
127-351 |
5.26e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 127 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALekEQKLQNDFAEKERKLQETQM-STTSKLEEAE 205
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELeELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 206 HKLQTLQTALEKTRTELFDLKTKYDEettAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQiqkap 285
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRG---NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE----- 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110815859 286 dvaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLE 351
Cdd:COG4913 381 --------------EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
58-355 |
5.29e-08 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 55.85 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 58 EDLRKQVAPLL---KSFQGEIDALSKRSKEAEAafltvykrlIDVPDPVPA---LDVGQQLEIKVQRLHDIETENQKLRE 131
Cdd:pfam05622 17 HELDQQVSLLQeekNSLQQENKKLQERLDQLES---------GDDSGTPGGkkyLLLQKQLEQLQEENFRLETARDDYRI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 132 TLEEYNKEFAE--VKNQEVT-----IKALKEKIREYEQTLK--SQAETIALEKEQKLQ--NDFAEKERKLQETQ---MST 197
Cdd:pfam05622 88 KCEELEKEVLElqHRNEELTslaeeAQALKDEMDILRESSDkvKKLEATVETYKKKLEdlGDLRRQVKLLEERNaeyMQR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 198 TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLEranQRAEVAQREAETL---REQLSSANHS 274
Cdd:pfam05622 168 TLQLEEELKKANALRGQLETYKRQVQELHGKLSEESK-KADKLEFEYKKLE---EKLEALQKEKERLiieRDTLRETNEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 275 LQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE----NSASQISQLEQQLNAKNSTLKQL 350
Cdd:pfam05622 244 LRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLgqegSYRERLTELQQLLEDANRRKNEL 323
|
....*
gi 110815859 351 EEKLK 355
Cdd:pfam05622 324 ETQNR 328
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
141-380 |
8.26e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 141 AEVKNQEVTIKALKEKIREYEQTLKSQAETI--ALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQTALEKT 218
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEkaLLKQLAALERRIAALARRIRALE----QELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 219 RTELFDLKTKYDE-----ETTAKADEIEMIM--TDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAiev 291
Cdd:COG4942 96 RAELEAQKEELAEllralYRLGRQPPLALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 292 ltRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRensaSQISQLEQQLNAKNSTLKQLEEKLKGQAdyEEVKKELNTLK 371
Cdd:COG4942 173 --RAELEALLAELEEERAALEALKAERQKLLARLE----KELAELAAELAELQQEAEELEALIARLE--AEAAAAAERTP 244
|
....*....
gi 110815859 372 SMEFAPSEG 380
Cdd:COG4942 245 AAGFAALKG 253
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
15-316 |
1.22e-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: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 15 FDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfltv 92
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELesKLDELAEELAELEEKLEELKEELESLEAELEELEAE---- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 93 ykrlidvpdpvpaldvgqqleikvqrLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIA 172
Cdd:TIGR02168 367 --------------------------LEELESRLEELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDRRE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 173 LEKEQKLQNDFAEKERKLQETQMSTTSK---LEEAEHKLQTLQTALEKTRTELFDLKTKYDeETTAKADEIEMIMTDLER 249
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAELEELeeeLEELQEELERLEEALEELREELEEAEQALD-AAERELAQLQARLDSLER 496
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110815859 250 ANQRAEVAQREAETLREQLSSANHSLQLASQIqkapdvaIEVLTRSSLEVELAAKEREIAQLVEDVQ 316
Cdd:TIGR02168 497 LQENLEGFSEGVKALLKNQSGLSGILGVLSEL-------ISVDEGYEAAIEAALGGRLQAVVVENLN 556
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
67-373 |
1.69e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 67 LLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVpdpvpalDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ 146
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELREL-------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAE 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 147 EvtIKALKEKIREYEQTLKSQAETiaLEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKLQTLQ-TALEKTRTELFDL 225
Cdd:PRK03918 526 E--YEKLKEKLIKLKGEIKSLKKE--LEKLEELKKKLAELEKKLDELE----EELAELLKELEELGfESVEELEERLKEL 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 226 KTKYDEETTAKADEIEmimtdLERANQRAEVAQREAETLREQLSSANHSLQLASQiqkapdvAIEVLTRSSLEVELAAKE 305
Cdd:PRK03918 598 EPFYNEYLELKDAEKE-----LEREEKELKKLEEELDKAFEELAETEKRLEELRK-------ELEELEKKYSEEEYEELR 665
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110815859 306 REIAQLVEDVQRLQAsltklrensasQISQLEQQLNAKNSTLKQLEEKLKgqaDYEEVKKELNTLKSM 373
Cdd:PRK03918 666 EEYLELSRELAGLRA-----------ELEELEKRREEIKKTLEKLKEELE---EREKAKKELEKLEKA 719
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
82-370 |
2.52e-06 |
|
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: 50.73 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 82 SKEAEAAFLTVYKRLIDVPDPVPALDVGQQLEIKVQRLHDIETE--NQKLRETLEEYNKEFAEVKNQEVTIKALKEKIRE 159
Cdd:COG5185 221 LLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVEQNTDlrLEKLGENAESSKRLNENANNLIKQFENTKEKIAE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 160 YEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYD-EETTAKAD 238
Cdd:COG5185 301 YTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSEELD 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 239 -----------EIEMIMTDLERANQRAE--------VAQREAETLREQLSSANHSLQLASQIQKA-------PDVAIEVL 292
Cdd:COG5185 381 sfkdtiestkeSLDEIPQNQRGYAQEILatledtlkAADRQIEELQRQIEQATSSNEEVSKLLNEliselnkVMREADEE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 293 TRSSLEVELAAKEREIAQ----LVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLK--GQADYEEVKKE 366
Cdd:COG5185 461 SQSRLEEAYDEINRSVRSkkedLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKdfMRARGYAHILA 540
|
....
gi 110815859 367 LNTL 370
Cdd:COG5185 541 LENL 544
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
110-283 |
3.05e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERK 189
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAE---LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 190 LQETQMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAK----ADEIEMIMTDLERANQRAEVAQREAETLR 265
Cdd:COG4717 151 LEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEELE 226
|
170
....*....|....*...
gi 110815859 266 EQLSSANHSLQLASQIQK 283
Cdd:COG4717 227 EELEQLENELEAAALEER 244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
110-270 |
4.02e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERK 189
Cdd:COG4913 274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 190 LQETQmsttSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 269
Cdd:COG4913 354 LEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
.
gi 110815859 270 S 270
Cdd:COG4913 430 S 430
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
151-353 |
1.68e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 48.09 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 151 KALKEKIREYEQTLKSQAETIALEKEQ-KLQNDFAEKERKL-----QETQMSTTSKLEEAE-HKLQTLQT---------- 213
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKngeniARKQNKYDELVEEAKtIKAEIEELtdellnlvmd 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 214 ------ALEKTRTELFDLKTKYD-----EETTAKADEIEMIMTDLERANQRaevaqreAETLREQLSSANHSL-QLASQI 281
Cdd:PHA02562 250 iedpsaALNKLNTAAAKIKSKIEqfqkvIKMYEKGGVCPTCTQQISEGPDR-------ITKIKDKLKELQHSLeKLDTAI 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110815859 282 QKAPDVAIEVLTRSS----LEVELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLNAKNSTLKQLEEK 353
Cdd:PHA02562 323 DELEEIMDEFNEQSKklleLKNKISTNKQSLITLVDKAKKVKAAIEELqaeFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
117-317 |
1.70e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 117 QRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQklqndfAEKERKLQETQmS 196
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREI------AELEAELERLD-A 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 197 TTSKLEEAEHKLQTLQTALEKTRTELFDLKTKY---DEETTAKADEIEMIMTDLERANQRAEVAQRE-AETLREQLSSAN 272
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDA 762
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 110815859 273 HSLQLASQIQKApdvaievltRSSLEVELAAKEREIAQLVEDVQR 317
Cdd:COG4913 763 VERELRENLEER---------IDALRARLNRAEEELERAMRAFNR 798
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
198-414 |
1.87e-05 |
|
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: 48.12 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 198 TSKLEEAEHKLQTLQTALEKTRTELFDLKTKydEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQlsSANHSLQL 277
Cdd:TIGR01612 1073 KEILEEAEINITNFNEIKEKLKHYNFDDFGK--EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKK--SENYIDEI 1148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 278 ASQIQKAPDVAIEVLTRSSLEvELAAKEREIA-------QLVEDVQRLQASLTKLRENSASqisqLEQQLNAKNSTLKQL 350
Cdd:TIGR01612 1149 KAQINDLEDVADKAISNDDPE-EIEKKIENIVtkidkkkNIYDEIKKLLNEIAEIEKDKTS----LEEVKGINLSYGKNL 1223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110815859 351 EEKLKGQADyEEVKKELNTLKSMEfAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSD 414
Cdd:TIGR01612 1224 GKLFLEKID-EEKKKSEHMIKAME-AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDD 1285
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
110-372 |
2.03e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEfaeVKNQEVTIKALKEKIreyeQTLKSQAETIALEKEQKLQNDFAE---- 185
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLSEKQKE---LEQNNKKIKELEKQL----NQLKSEISDLNNQKEQDWNKELKSelkn 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 186 KERKLQETQmSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQraevaqrEAETLR 265
Cdd:TIGR04523 319 QEKKLEEIQ-NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ-------EIKNLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 266 EQLSSANHSLQLASQIQKAPDVAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAKNS 345
Cdd:TIGR04523 391 SQINDLESKIQNQEKLNQQKDEQIK-----KLQQEKELLEKEIERLKETIIKNNSEIKDLTN----QDSVKELIIKNLDN 461
|
250 260
....*....|....*....|....*..
gi 110815859 346 TLKQLEEKLKgqadyeEVKKELNTLKS 372
Cdd:TIGR04523 462 TRESLETQLK------VLSRSINKIKQ 482
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
187-373 |
2.05e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 187 ERKLQETQMSTT---SKLEEAEHKLQTLQTALE--KTRTELFDLktkyDEETTAKADEIEMIMTDLERANQRAEVAQREA 261
Cdd:COG3206 167 ELRREEARKALEfleEQLPELRKELEEAEAALEefRQKNGLVDL----SEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 262 ETLREQLSSanhSLQLASQIQKAPDVAIEVLTRSSLEVELA--------------AKEREIA----QLVEDVQRLQASLT 323
Cdd:COG3206 243 AALRAQLGS---GPDALPELLQSPVIQQLRAQLAELEAELAelsarytpnhpdviALRAQIAalraQLQQEAQRILASLE 319
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 110815859 324 KLRENSASQISQLEQQLNAKNSTLKQLEEKlkgQADYEEVKKELNTLKSM 373
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPEL---EAELRRLEREVEVAREL 366
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
101-355 |
2.16e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.98 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 101 DPVPALDVGQQLEiKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK-SQAETIALEKeqkl 179
Cdd:PRK11281 34 DLPTEADVQAQLD-ALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRqAQAELEALKD---- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 180 QNDFAEKER--KLQETQMSttSKLEEAEHKLQTLQTALEKTRTELFDLKTKydeettakadeiemimtdLERA-NQRAEV 256
Cdd:PRK11281 109 DNDEETRETlsTLSLRQLE--SRLAQTLDQLQNAQNDLAEYNSQLVSLQTQ------------------PERAqAALYAN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 257 AQREAEtLREQLSS--ANHSLQLASQIQKapdvaievltrssLEVELAAKEREIA---QLVEDVQRLQASLTKLRENSAS 331
Cdd:PRK11281 169 SQRLQQ-IRNLLKGgkVGGKALRPSQRVL-------------LQAEQALLNAQNDlqrKSLEGNTQLQDLLQKQRDYLTA 234
|
250 260 270
....*....|....*....|....*....|.
gi 110815859 332 QISQLEQQL-------NAKNstLKQLEEKLK 355
Cdd:PRK11281 235 RIQRLEHQLqllqeaiNSKR--LTLSEKTVQ 263
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
127-532 |
2.45e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 127 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEH 206
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK 1552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 207 KLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMImtDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPD 286
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA--EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 287 VAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKE 366
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 367 lntlksmefapsegaGTQDSTKPLEVLLLEKNRSLQSENATlrisnsdlsgRCAELQIHLTEATAKAVEQKELIARLEQD 446
Cdd:PTZ00121 1711 ---------------EAEEKKKAEELKKAEEENKIKAEEAK----------KEAEEDKKKAEEAKKDEEEKKKIAHLKKE 1765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 447 LSTIQSIQRPDAEGASEQGLEKIPEPIKEATALFYGPSMSSSGTLPEGQVDSLLsIISSQRERFRTRNQELEAESRMAQH 526
Cdd:PTZ00121 1766 EEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNL-VINDSKEMEDSAIKEVADSKNMQLE 1844
|
....*.
gi 110815859 527 TIQALQ 532
Cdd:PTZ00121 1845 EADAFE 1850
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
110-372 |
2.52e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.71 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 110 QQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQAETIALEKeQKLQNDFAE 185
Cdd:TIGR04523 412 EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQdsvkELIIKNLDNTRESLETQLKVLSRSINKIK-QNLEQKQKE 490
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 186 KERKLQETQMST--TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAET 263
Cdd:TIGR04523 491 LKSKEKELKKLNeeKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEI 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 264 lrEQLSSANHSLqLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLEQQLNAK 343
Cdd:TIGR04523 571 --EELKQTQKSL-KKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKL----SSIIKNIKSKKNKL 643
|
250 260 270
....*....|....*....|....*....|
gi 110815859 344 NSTLKQLEEKLKG-QADYEEVKKELNTLKS 372
Cdd:TIGR04523 644 KQEVKQIKETIKEiRNKWPEIIKKIKESKT 673
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
233-448 |
2.63e-05 |
|
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: 47.07 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 233 TTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQiqkapdvAIEVLTR--SSLEVELAAKEREIAQ 310
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-------RIAALARriRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 311 LVEDVQRLQASLTKLRENSASQISQLEQQ---------LNAKNST--------LKQLEEKLKGQAD-YEEVKKELNTLKS 372
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLgrqpplallLSPEDFLdavrrlqyLKYLAPARREQAEeLRADLAELAALRA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110815859 373 mefapsEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGRCAELQIHLTEATAKAVEQKELIARLEQDLS 448
Cdd:COG4942 168 ------ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
232-452 |
3.12e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 232 ETTAKADEIEMIMTDLERANQRAEVAQREAETLR------EQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKE 305
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 306 REIAQLVEDVQRLQASLTKLREnsasQISQLEQQL-NAKNSTLKQLEEKLKG-QADYEEVKKELNTLKsmefapsEGAGT 383
Cdd:COG4913 302 AELARLEAELERLEARLDALRE----ELDELEAQIrGNGGDRLEQLEREIERlERELEERERRRARLE-------ALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110815859 384 QDSTKPLEVLLLEKNRSLQSENATlrisnsDLSGRCAELQIHLTEATAKAVEQKELIARLEQDLSTIQS 452
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLE------ALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
14-423 |
3.30e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 14 RFDLQQLQRELDATATV----LANRQDESEQSRKRLIEQSR----------EFKKNTPEDLRKQVAPLLKSFQGEIDALS 79
Cdd:pfam15921 144 RNQLQNTVHELEAAKCLkedmLEDSNTQIEQLRKMMLSHEGvlqeirsilvDFEEASGKKIYEHDSMSTMHFRSLGSAIS 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 80 KRSKEAEAAFLTVYKRLIDVPDPVPALDVGQQLEIKVQrlhdIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIRE 159
Cdd:pfam15921 224 KILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELL----LQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 160 YEQTLKSQAE---TIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTElfdlKTKYDEETTAK 236
Cdd:pfam15921 300 QLEIIQEQARnqnSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTE----RDQFSQESGNL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 237 ADEIEMIMTDLERANQRAEVAQREAETLREQlssanhslqlasqiQKAPDVAIEVLTRsslevELAAKEREiaqlvedVQ 316
Cdd:pfam15921 376 DDQLQKLLADLHKREKELSLEKEQNKRLWDR--------------DTGNSITIDHLRR-----ELDDRNME-------VQ 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 317 RLQASLTKLRENSASQISQLEQQLNAKNSTLKQ---LEEKLKGQADYEEVKKELNTLKSMEFAPSEgagtqDSTKPLEVL 393
Cdd:pfam15921 430 RLEALLKAMKSECQGQMERQMAAIQGKNESLEKvssLTAQLESTKEMLRKVVEELTAKKMTLESSE-----RTVSDLTAS 504
|
410 420 430
....*....|....*....|....*....|
gi 110815859 394 LLEKNRSLQSENATLRISNSDLSGRCAELQ 423
Cdd:pfam15921 505 LQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
16-288 |
3.48e-05 |
|
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: 46.68 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 16 DLQQLQRELDAtatvLANRQDESEQSRKRLIEQsrefkkntpedlrkqvaplLKSFQGEIDALSKRSKEAEaafltvykr 95
Cdd:COG4942 28 ELEQLQQEIAE----LEKELAALKKEEKALLKQ-------------------LAALERRIAALARRIRALE--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 96 lidvpdpvpaldvgQQLEIKVQRLHDIETENQKLRETLEEYNKEFAevknqEVTIKALKEKIREYEQTLKSQAETIALEK 175
Cdd:COG4942 76 --------------QELAALEAELAELEKEIAELRAELEAQKEELA-----ELLRALYRLGRQPPLALLLSPEDFLDAVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 176 EQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAE 255
Cdd:COG4942 137 RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
250 260 270
....*....|....*....|....*....|...
gi 110815859 256 VAQREAETLREQLSSANHSLQLASQIQKAPDVA 288
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
174-554 |
5.97e-05 |
|
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: 46.27 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 174 EKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRtELFDLKTKYDEETTAKADEIEMIMTDLERANQR 253
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN-EKESQLADAREVISCLKNELSELRRQIQRAELE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 254 AEVAQREAETLREQ-----------------LSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKERE-IAQLVEDV 315
Cdd:pfam05557 127 LQSTNSELEELQERldllkakaseaeqlrqnLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELArIPELEKEL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 316 QRLQASLTKLRENSASqISQLEQQLNAKNSTLKQLE----EKLKGQADYEEVKKELNTLKSMEFA-------PSEGAGTQ 384
Cdd:pfam05557 207 ERLREHNKHLNENIEN-KLLLKEEVEDLKRKLEREEkyreEAATLELEKEKLEQELQSWVKLAQDtglnlrsPEDLSRRI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 385 DSTKPLEVLLLEKNRSLQSENATLRISNSDLSGRCAELQIHLTEATAKAVEQKELIARLEQDLSTI--------QSIQRP 456
Cdd:pfam05557 286 EQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLtkerdgyrAILESY 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 457 DAEGASEQGLEKIPEPIKEATALFygPSMSSSGTLPEGQVDSLLSIISSQRERFRT--------RNQELEAESRMAQHTI 528
Cdd:pfam05557 366 DKELTMSNYSPQLLERIEEAEDMT--QKMQAHNEEMEAQLSVAEEELGGYKQQAQTlerelqalRQQESLADPSYSKEEV 443
|
410 420
....*....|....*....|....*.
gi 110815859 529 QALQSELDSLRADNIKLFEKIKFLQS 554
Cdd:pfam05557 444 DSLRRKLETLELERQRLREQKNELEM 469
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
72-447 |
7.50e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 72 QGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYnkefaevKNQEVTIK 151
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-------RELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 152 ALKEKIREYEQTLKSQAETIALEKEQKLQnDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKtkyDE 231
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA---LE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 232 ETTAKADEIEMIMT-----------DLERANQRAEVAQ-------REAETLREQLSSANHSLQLASQIQKAPDVAIEVLT 293
Cdd:COG4717 243 ERLKEARLLLLIAAallallglggsLLSLILTIAGVLFlvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 294 R--SSLEVELAAKEREIAQLVEDVQRLQASLTKLRE-NSASQISQLEQQLN-----AKNSTLKQLEEKLKGQADYEEVKK 365
Cdd:COG4717 323 EllAALGLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAallaeAGVEDEEELRAALEQAEEYQELKE 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 366 ELNTLKSmEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGRCAELQIHLteataKAVEQKELIARLEQ 445
Cdd:COG4717 403 ELEELEE-QLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL-----EQLEEDGELAELLQ 476
|
..
gi 110815859 446 DL 447
Cdd:COG4717 477 EL 478
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
11-301 |
7.52e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.22 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 11 YWKRFDLQQLQRELDATaTVLANRQDESEQSRKRLIE---QSREFK--KNTPEDLRKQVAPLLKSFQGEIDALSKrSKEA 85
Cdd:COG5022 851 FGRSLKAKKRFSLLKKE-TIYLQSAQRVELAERQLQElkiDVKSISslKLVNLELESEIIELKKSLSSDLIENLE-FKTE 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 86 EAAFLTVYKRLIDVPDPvPALDVGQQLEikVQRLHdieTENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK 165
Cdd:COG5022 929 LIARLKKLLNNIDLEEG-PSIEYVKLPE--LNKLH---EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELA 1002
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 166 S--------QAETIALEKEQK----LQNDF-------AEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLK 226
Cdd:COG5022 1003 ElskqygalQESTKQLKELPVevaeLQSASkiissesTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQ 1082
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110815859 227 TKYDEETTAKADEIEmiMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQI-QKAPDVAIEVLTRSSLEVEL 301
Cdd:COG5022 1083 LYQLESTENLLKTIN--VKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLsQLVNTLEPVFQKLSVLQLEL 1156
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
126-447 |
1.10e-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: 45.51 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 126 NQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQA-ETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 204
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 205 EHK-LQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLE--RANQRAE--VAQREAETLREQLSSANHSLQlaS 279
Cdd:pfam07111 138 SQReLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkRAGEAKQlaEAQKEAELLRKQLSKTQEELE--A 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 280 QIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQ---------ASLTKLRENSASQISQL-EQQLNAKNSTLKQ 349
Cdd:pfam07111 216 QVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQedradlqatVELLQVRVQSLTHMLALqEEELTRKIQPSDS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 350 LEEKLKgqadyEEVKKELNTLKSMEFA-----PSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGRCAE--- 421
Cdd:pfam07111 296 LEPEFP-----KKCRSLLNRWREKVFAlmvqlKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEvev 370
|
330 340 350
....*....|....*....|....*....|...
gi 110815859 422 -------LQIHLTEATAKAVEQKELIARLEQDL 447
Cdd:pfam07111 371 ermsakgLQMELSRAQEARRRQQQQTASAEEQL 403
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
196-389 |
1.12e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 196 STTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL 275
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 276 QLASQIQKAPDV---------------AIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQ 338
Cdd:COG3883 96 YRSGGSVSYLDVllgsesfsdfldrlsALSKIADADADLleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 110815859 339 QLNAKNSTLKQLEEKLK-GQADYEEVKKELNTLKSMEFAPSEGAGTQDSTKP 389
Cdd:COG3883 176 QQAEQEALLAQLSAEEAaAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
58-250 |
1.14e-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: 44.67 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 58 EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLTVYKRLIDvpdpvpalDVGQQLEIKVQRLHDI-ETENQKL-RETLEE 135
Cdd:cd22656 113 EEAKKTIKALLDDLLKEAKKYQDKAAKVVDK-LTDFENQTE--------KDQTALETLEKALKDLlTDEGGAIaRKEIKD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 136 YNKEFAevKNQEVTIKALKEKIREYEQTLKSQAETIAleKEQKLQNDFaekerKLQETQM-STTSKLEEAEHKLQTLQTA 214
Cdd:cd22656 184 LQKELE--KLNEEYAAKLKAKIDELKALIADDEAKLA--AALRLIADL-----TAADTDLdNLLALIGPAIPALEKLQGA 254
|
170 180 190
....*....|....*....|....*....|....*.
gi 110815859 215 LEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERA 250
Cdd:cd22656 255 WQAIATDLDSLKDLLEDDIS-KIPAAILAKLELEKA 289
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
18-237 |
1.81e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 18 QQLQRELDATATVLANRQDESEQSRKRLIEQS---REFKKNT----PEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFL 90
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEaalEEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 91 TVYKRLIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAET 170
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 171 ---IALEKEQKLQNDFAEKERKLQEtqmsttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKA 237
Cdd:COG3206 321 eleALQAREASLQAQLAQLEARLAE--------LPELEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
123-553 |
2.11e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 123 ETENQKLRETLEEYNKEFAEVKnqevtikalkEKIREYEqtlkSQAETiALEKEQKLQNDFAEKERKLQETQmsttsKLE 202
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELD----------EEIERYE----EQREQ-ARETRDEADEVLEEHEERREELE-----TLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 203 EAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQ 282
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 283 KAPDVAIEVLTRSSLEVELAAKE-REIAQLVEDvqRLQASLTKLREnSASQISQLEQQLNAKNSTLKQLEEKLKGQADY- 360
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEElREEAAELES--ELEEAREAVED-RREEIEELEEEIEELRERFGDAPVDLGNAEDFl 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 361 EEVKKELN-----------TLKSMEFAPSEGAGTQDSTK------PLE----VLLLEKNR----SLQSENATLRISNSDL 415
Cdd:PRK02224 415 EELREERDelrereaeleaTLRTARERVEEAEALLEAGKcpecgqPVEgsphVETIEEDRerveELEAELEDLEEEVEEV 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 416 SGRCAELQihlteataKAVEQKELIARLEQDLSTIQSIQRPDAEGASEQGlEKIPEPIKEATALfygpsmSSSGTLPEGQ 495
Cdd:PRK02224 495 EERLERAE--------DLVEAEDRIERLEERREDLEELIAERRETIEEKR-ERAEELRERAAEL------EAEAEEKREA 559
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 496 VDSLLSIISSQRERFRTRNQELEA--ESRMAQHTIQALQSELDSLRADNIKLFEKIKFLQ 553
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNSKLAElkERIESLERIRTLLAAIADAEDEIERLREKREALA 619
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
25-358 |
2.28e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 25 DATATVLANRQDE----SEQSRKRLIEQ--SREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRlid 98
Cdd:PRK02224 306 DADAEAVEARREEledrDEELRDRLEECrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDR--- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 99 vPDPVPALDvgQQLEIKVQRLHDIETEnqklRETLEEYNKEFAEVKNqevtikALKEKIREYEQTLKSQAETIALEKEQK 178
Cdd:PRK02224 383 -REEIEELE--EEIEELRERFGDAPVD----LGNAEDFLEELREERD------ELREREAELEATLRTARERVEEAEALL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 179 LQNDFAEKERKLQETQMSTTskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAK--ADEIEMIMTDLERANQRAEV 256
Cdd:PRK02224 450 EAGKCPECGQPVEGSPHVET--IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaEDRIERLEERREDLEELIAE 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 257 AQREAETLREQLSSANHSLQ-LASQIQKAPDVAIEVLTRS-SLEVELAAKEREIAQLVEDVQRLQ--ASLTKLRENSASQ 332
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAeLEAEAEEKREAAAEAEEEAeEAREEVAELNSKLAELKERIESLEriRTLLAAIADAEDE 607
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 110815859 333 ISQLEQQ--------------LNAKNSTLKQLEEKLKGQA 358
Cdd:PRK02224 608 IERLREKrealaelnderrerLAEKRERKRELEAEFDEAR 647
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
108-352 |
3.72e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 108 VGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIalekeQKLQNDFAEKE 187
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI-----RELEERIEELK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 188 RKLQ--ETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLR 265
Cdd:PRK03918 273 KEIEelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE-KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 266 EQLSSANHSLQLASQIqKAPDVAIEvltrsSLEVELAAKERE-IAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKN 344
Cdd:PRK03918 352 KRLEELEERHELYEEA-KAKKEELE-----RLKKRLTGLTPEkLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK 425
|
....*...
gi 110815859 345 STLKQLEE 352
Cdd:PRK03918 426 KAIEELKK 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
16-359 |
4.65e-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: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 16 DLQQLQRELDATATVLANRQDESEQSRKRLiEQSREFKKNTPEDLRkqvaplLKSFQGEIDALSKRSKEAEAAFLTVykr 95
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERR-EALQRLAEYSWDEID------VASAEREIAELEAELERLDASSDDL--- 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 96 lidvpdpvpaldvgQQLEikvQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKSQAETIALEK 175
Cdd:COG4913 688 --------------AALE---EQLEELEAELEELEEELDELKGEIGRLEKE---LEQAEEELDELQDRLEAAEDLARLEL 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 176 EQKLQNDFAEKERKLQETQMSttsklEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLERANQ-RA 254
Cdd:COG4913 748 RALLEERFAAALGDAVERELR-----ENLEERIDALRARLNRAEEELERAMRAFNREWPAETAD---LDADLESLPEyLA 819
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 255 EVAQREAETL-------REQLSSANHS--LQLASQIQKAPDVAIEVLTR--SSLE---------VELAAKEREiaqlVED 314
Cdd:COG4913 820 LLDRLEEDGLpeyeerfKELLNENSIEfvADLLSKLRRAIREIKERIDPlnDSLKripfgpgryLRLEARPRP----DPE 895
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 110815859 315 VQRLQASLTKLRENSASQIsqlEQQLNAKNSTLKQLEEKLKGQAD 359
Cdd:COG4913 896 VREFRQELRAVTSGASLFD---EELSEARFAALKRLIERLRSEEE 937
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
119-446 |
5.39e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 119 LHDIETENQKLRETLEEYNKEFAEVKN----------QEVTIKALKEKIREYEQTLKSQAETIALEKEQKlqndfaEKER 188
Cdd:pfam10174 201 LDQKEKENIHLREELHRRNQLQPDPAKtkalqtviemKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDR------EEEI 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 189 KLQETQMSTTSKLeeaEHKLQTLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQREAETLR 265
Cdd:pfam10174 275 KQMEVYKSHSKFM---KNKIDQLKQELSKKESELLALQTKLETLTNQNSDckqHIEVLKESLTAKEQRAAILQTEVDALR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 266 EQLSS-----ANHSLQLASQIQKAPDVAIEVltrSSLEVELAAKEREIAQLVEDVQRLQASL---TKLRENSASQISQLE 337
Cdd:pfam10174 352 LRLEEkesflNKKTKQLQDLTEEKSTLAGEI---RDLKDMLDVKERKINVLQKKIENLQEQLrdkDKQLAGLKERVKSLQ 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 338 QQLNAKNSTLKQLEEKLkgqADYEEVKKELNTLKSMEfapsegagtqdstkplevlllekNRSLQSENATLRISNSDLSG 417
Cdd:pfam10174 429 TDSSNTDTALTTLEEAL---SEKERIIERLKEQRERE-----------------------DRERLEELESLKKENKDLKE 482
|
330 340
....*....|....*....|....*....
gi 110815859 418 RCAELQIHLTEATAKAVEQKELIARLEQD 446
Cdd:pfam10174 483 KVSALQPELTEKESSLIDLKEHASSLASS 511
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
117-259 |
5.54e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 117 QRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQTL---KSQAETIALEKEQklqnDFAEKERK 189
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELedleKEIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQKEI----ESLKRRIS 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110815859 190 LQETQMS-TTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTdlERANQRAEVAQR 259
Cdd:COG1579 107 DLEDEILeLMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA--EREELAAKIPPE 175
|
|
| ClyA_NheA-like |
cd22654 |
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This ... |
105-370 |
6.93e-04 |
|
Bacillus cereus non-hemolytic enterotoxin (Nhe) component A (NheA), and similar proteins; This model contains Bacillus cereus tripartite non-hemolytic enterotoxin (Nhe) component A (NheA), a member of the cytolysin A (ClyA) family of alpha pore-forming toxins (alpha-PFTs). Non-hemolytic enterotoxin (Nhe), despite its name, is hemolytic and able to lyse erythrocytes from various mammalian organisms. It consists of three proteins, NheA, NheB and NheC, encoded by one operon containing three genes nheA, nheB and nheC, respectively. Separately, these three proteins show no toxicity; maximal activity is seen only when all three components are presented. The NheB and NheC components are able to bind to cell membranes while NheA is not; NheC primes the host cell for the formation of ion permeable NheB/C pores. Binding of NheA to NheB/NheC is thought to be the final stage of pore formation. Structure of NheA shows an elongated, almost entirely alpha-helical protein with an enlarged "head" domain compared with other cytolysins, displaying on its surface an enlarged beta-tongue which is of amphipathic rather than hydrophobic nature. It has been proposed that NheA could even form beta-barrel pores.
Pssm-ID: 439152 [Multi-domain] Cd Length: 333 Bit Score: 42.25 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 105 ALDVGQQLEIKVQRLHDIeTENQKL-----RETLEEYNKEFAEVkNQEvtIKALKEKIREYEQTLKSQAETIALEKEQKl 179
Cdd:cd22654 18 ALVILKQPNVKIEAMPSL-TNHQQTakenvREWLDEYNPKLIDL-NQD--MINFSQRFNNYYDKLYDLAGKINEDEQAK- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 180 qNDFAEKERKLQEtqmsttskleeaehKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANqrAEVAQr 259
Cdd:cd22654 93 -EDFLNGINKLQS--------------QLQTIQNSMEQTSSNLNRFKTLLDADSKNFSTDAKKAIDSLSGSN--GEIAQ- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 260 eaetLREQLSSANHSLQ-------------------LASQI---------QKAPDVAI------EVLTRSSLEVELAAKe 305
Cdd:cd22654 155 ----LRTQIKTINDEIQeeltkilnrpievgdgsinIGKQVftitittatTKTVDVTSigglinGIGNASDDEVKEAAN- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110815859 306 rEIAQLVEDVQRLQASLTKLrENSASQISQLEQQLNAKNSTLKqleeklKGQADYEEVKKELNTL 370
Cdd:cd22654 230 -KIQQKQKELVDLIKKLSDA-EIQATQLTLVEDQVNGFTELIK------RQIATLENLVEDWEML 286
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
118-227 |
8.51e-04 |
|
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: 41.93 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 118 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAET---IALEKEQKLQNDFA---EKERKLQ 191
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELDrakEKLKKLL 217
|
90 100 110
....*....|....*....|....*....|....*.
gi 110815859 192 ETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKT 227
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT 253
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
106-373 |
9.54e-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: 42.65 E-value: 9.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 106 LDVGQQLEIKVQRLHDIETENQKLRETL--EEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQA----ETIA--LEKEQ 177
Cdd:TIGR00618 628 QDVRLHLQQCSQELALKLTALHALQLTLtqERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkEMLAqcQTLLR 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 178 KLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRtELFDLKTKYDEETTAKADE----IEMIMTDLERANQR 253
Cdd:TIGR00618 708 ELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELM-HQARTVLKARTEAHFNNNEevtaALQTGAELSHLAAE 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 254 AEVAQREAETLREQLSsanhslQLASQIQKAPDVAIEVLTrssLEVELAAKEREiaqlvedvqrlqASLTKLRENSASQI 333
Cdd:TIGR00618 787 IQFFNRLREEDTHLLK------TLEAEIGQEIPSDEDILN---LQCETLVQEEE------------QFLSRLEEKSATLG 845
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 110815859 334 sQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSM 373
Cdd:TIGR00618 846 -EITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQI 884
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
21-246 |
1.19e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 21 QRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaafltvykrlidvP 100
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE-------------E 1658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 101 DPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKsqAETIALEKEQKLQ 180
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAEEAK 1736
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110815859 181 NDFAEKERKLQETQmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD 246
Cdd:PTZ00121 1737 KEAEEDKKKAEEAK-----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
110-356 |
1.28e-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: 42.13 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 110 QQLEIKVQRLHDietENQKLRETLEEYNKEFAEVKNQEVT-----IKALKEKIREYEQTLKSQAETIALEKEQKLQNdfA 184
Cdd:pfam12128 649 KNARLDLRRLFD---EKQSEKDKKNKALAERKDSANERLNsleaqLKQLDKKHQAWLEEQKEQKREARTEKQAYWQV--V 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 185 EKERKLQETQMSTTSKLEEAEHKLQtlQTALEKTRTElfDLKTK-YDEETTAK-ADEIEMIMTDLERANQRAEVAQREAE 262
Cdd:pfam12128 724 EGALDAQLALLKAAIAARRSGAKAE--LKALETWYKR--DLASLgVDPDVIAKlKREIRTLERKIERIAVRRQEVLRYFD 799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 263 TLREQLSSANHSLQlasqiqkapdvaievltrssleVELAAKEREIAQLVEDVQRLQASlTKLRensasqISQLEQQLNA 342
Cdd:pfam12128 800 WYQETWLQRRPRLA----------------------TQLSNIERAISELQQQLARLIAD-TKLR------RAKLEMERKA 850
|
250
....*....|....
gi 110815859 343 KNSTLKQLEEKLKG 356
Cdd:pfam12128 851 SEKQQVRLSENLRG 864
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
105-529 |
1.29e-03 |
|
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: 42.04 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 105 ALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKefaevknqevtikALKEKIREYEQTLKSqaetiaLEKEQKLQNDFA 184
Cdd:pfam05557 36 ASALKRQLDRESDRNQELQKRIRLLEKREAEAEE-------------ALREQAELNRLKKKY------LEALNKKLNEKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 185 EKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEettakadeiemimtdleranQRAEVAqrEAETL 264
Cdd:pfam05557 97 SQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDL--------------------LKAKAS--EAEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 265 REQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQASLTKLRENSASqISQLEQQLNAK 343
Cdd:pfam05557 155 RQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELArIPELEKELERLREHNKHLNENIEN-KLLLKEEVEDL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 344 NSTLKQLE----EKLKGQADYEEVKKELNTLKSMEFA-------PSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISN 412
Cdd:pfam05557 234 KRKLEREEkyreEAATLELEKEKLEQELQSWVKLAQDtglnlrsPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 413 SDLSGRCAELQIHLTEATAKAVEQKELIARLEQDLSTI--------QSIQRPDAEGASEQGLEKIPEPIKEAT------- 477
Cdd:pfam05557 314 RELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLtkerdgyrAILESYDKELTMSNYSPQLLERIEEAEdmtqkmq 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 478 --------------------------------ALFYGPSMSSSGTLPEGqVDSL---LSIISSQRERFRTRNQELeaESR 522
Cdd:pfam05557 394 ahneemeaqlsvaeeelggykqqaqtlerelqALRQQESLADPSYSKEE-VDSLrrkLETLELERQRLREQKNEL--EME 470
|
....*..
gi 110815859 523 MAQHTIQ 529
Cdd:pfam05557 471 LERRCLQ 477
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
130-446 |
1.34e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 130 RETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETialekEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQ 209
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR-----KKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 210 TLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLaSQIQKAPDVAI 289
Cdd:TIGR00606 312 RTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLEL-DGFERGPFSER 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 290 EVLTRSSLEVE-LAAKEREIAQLVEDVQRLQASLTKlrensasQISQLEQQLNAKNSTLKQLEEKL-KGQADYEEVKKEL 367
Cdd:TIGR00606 391 QIKNFHTLVIErQEDEAKTAAQLCADLQSKERLKQE-------QADEIRDEKKGLGRTIELKKEILeKKQEELKFVIKEL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 368 NTL---------KSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGRCAELQIHLTEATakaveQKE 438
Cdd:TIGR00606 464 QQLegssdrileLDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRT-----QME 538
|
....*...
gi 110815859 439 LIARLEQD 446
Cdd:TIGR00606 539 MLTKDKMD 546
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
122-358 |
1.58e-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: 41.75 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 122 IETENQKLRETLEEYNKEFAEVKNQevtikaLKEKIREYEQTLKSQAETIALEKEQ---------KLQNDFAEKERKLQE 192
Cdd:pfam12128 274 IASRQEERQETSAELNQLLRTLDDQ------WKEKRDELNGELSAADAAVAKDRSElealedqhgAFLDADIETAAADQE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 193 TQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDLE-----RANQRAE---VAQREAETL 264
Cdd:pfam12128 348 QLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN---NRDIAGIKDKLAkireaRDRQLAVaedDLQALESEL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 265 REQLSSANHSL-----QLASQI------QKAPDVAIEVLTRSSLEVELAAKEREIAQL----VEDVQRLQASLTKLRENS 329
Cdd:pfam12128 425 REQLEAGKLEFneeeyRLKSRLgelklrLNQATATPELLLQLENFDERIERAREEQEAanaeVERLQSELRQARKRRDQA 504
|
250 260
....*....|....*....|....*....
gi 110815859 330 ASQISQLEQQLNAKNSTLKQLEEKLKGQA 358
Cdd:pfam12128 505 SEALRQASRRLEERQSALDELELQLFPQA 533
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
121-353 |
2.26e-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: 41.48 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 121 DIETENQKLRE---TLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKSQaETIALEKEQKLQNdFAEKERKLQET 193
Cdd:COG3096 355 DLEELTERLEEqeeVVEEAAEQLAEAEARleaaEEEVDSLKSQLADYQQALDVQ-QTRAIQYQQAVQA-LEKARALCGLP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 194 QMSttskLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKA--DE----IEMIMTDLER--ANQRAE---------- 255
Cdd:COG3096 433 DLT----PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRqfEKayelVCKIAGEVERsqAWQTARellrryrsqq 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 256 -VAQReAETLREQLSSANhslQLASQIQKAPDVAIEVLTRSSLEVELAAK-EREIAQLVEDVQRLQASLTKLREnsasQI 333
Cdd:COG3096 509 aLAQR-LQQLRAQLAELE---QRLRQQQNAERLLEEFCQRIGQQLDAAEElEELLAELEAQLEELEEQAAEAVE----QR 580
|
250 260
....*....|....*....|
gi 110815859 334 SQLEQQLNAKNSTLKQLEEK 353
Cdd:COG3096 581 SELRQQLEQLRARIKELAAR 600
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
128-435 |
2.33e-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: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 128 KLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTL--KSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAE 205
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKlaQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 206 HKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAP 285
Cdd:pfam02463 310 VDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 286 DVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKK 365
Cdd:pfam02463 390 AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK 469
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 366 ELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGRCAELQIHLTEATAKAVE 435
Cdd:pfam02463 470 SEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVE 539
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
127-342 |
2.47e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 127 QKLRETLEEYNKEFAEVkNQEVTIKALKEKIREYEQTLKSQAETiaLEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEH 206
Cdd:PRK10929 82 AELRQQLNNERDEPRSV-PPNMSTDALEQEILQVSSQLLEKSRQ--AQQEQDRAREISDSLSQLPQQQTEARRQLNEIER 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 207 KLQTL--------QTALEKTRTELFDLKtkydeettAKADEIEMIMTDL----ERANQRAEVAQREAETLREQLSSANHs 274
Cdd:PRK10929 159 RLQTLgtpntplaQAQLTALQAESAALK--------ALVDELELAQLSAnnrqELARLRSELAKKRSQQLDAYLQALRN- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 275 lQLASQIQKAPDVAIEvltrsslEVELAAKE---------------REIAQ-LVEDVQRLQASLTKLREnSASQISQLEQ 338
Cdd:PRK10929 230 -QLNSQRQREAERALE-------STELLAEQsgdlpksivaqfkinRELSQaLNQQAQRMDLIASQQRQ-AASQTLQVRQ 300
|
....
gi 110815859 339 QLNA 342
Cdd:PRK10929 301 ALNT 304
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
113-355 |
3.06e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 113 EIKVQRLhDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLksQAETIALEKEQKLQNDFAEKERKLQE 192
Cdd:COG1340 75 ELKEERD-ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ--QTEVLSPEEEKELVEKIKELEKELEK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 193 TQmsttsKLEEAEHKLQTLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLeranqraevaQREAETLREQLSSAN 272
Cdd:COG1340 152 AK-----KALEKNEKLKELRAELKELRKEAEEIHKKI-KELAEEAQELHEEMIEL----------YKEADELRKEADELH 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 273 HSLQLASQiqkapdvaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASqiSQLEQQLNAKNSTLKQLEE 352
Cdd:COG1340 216 KEIVEAQE-------------------KADELHEEIIELQKELRELRKELKKLRKKQRA--LKREKEKEELEEKAEEIFE 274
|
...
gi 110815859 353 KLK 355
Cdd:COG1340 275 KLK 277
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
122-352 |
3.24e-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: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 122 IETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYeqtlKSQAETIALEKEQKLqndFAEKERKLQETQMSTTSKL 201
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKE---LEEAEAALEEF----RQKNGLVDLSEEAKL---LLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 202 EEAEHKLQTLQTALEKT----------------RTELFDLKTKYDEE-TTAKADEIEMIMTDLERANQRAEVAQREAETL 264
Cdd:COG3206 236 AEAEARLAALRAQLGSGpdalpellqspviqqlRAQLAELEAELAELsARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 265 REQLSSANHSLQLASQIQKApdvaIEVLTRSSLEveLAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLNAKN 344
Cdd:COG3206 316 ASLEAELEALQAREASLQAQ----LAQLEARLAE--LPELEAELRRLEREVEVARELYESLLQ----RLEEARLAEALTV 385
|
....*...
gi 110815859 345 STLKQLEE 352
Cdd:COG3206 386 GNVRVIDP 393
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
114-325 |
3.63e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 114 IKVQRLHdIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKSQAETIalekeQKLQNDFAEKERK 189
Cdd:PHA02562 197 IKTYNKN-IEEQRKKNGENIARKQNKYDELVEEAKTIKAeieeLTDELLNLVMDIEDPSAAL-----NKLNTAAAKIKSK 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 190 LQ----ETQMST--------TSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETtakadeiemimtdlERANQRAEvA 257
Cdd:PHA02562 271 IEqfqkVIKMYEkggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE--------------EIMDEFNE-Q 335
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110815859 258 QREAETLREQLSSANHSLQLASQIQKAPDVAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL 325
Cdd:PHA02562 336 SKKLLELKNKISTNKQSLITLVDKAKKVKAAIE-----ELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
246-544 |
4.17e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 40.27 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 246 DLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTR----------------SSLEVELAAKEREIA 309
Cdd:PLN02939 157 DLEKILTEKEALQGKINILEMRLSETDARIKLAAQEKIHVEILEEQLEKlrnellirgateglcvHSLSKELDVLKEENM 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 310 QLVEDVQRLQASLTKLRENSASqISQLEQQLNAKNSTLKQLEEKLkgQADYEEVKKeLNTLKsmefapsegagtQDStkp 389
Cdd:PLN02939 237 LLKDDIQFLKAELIEVAETEER-VFKLEKERSLLDASLRELESKF--IVAQEDVSK-LSPLQ------------YDC--- 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 390 levlLLEKNRSLQsenatlrisnsdlsgrcaelqiHLTEATAKAVEQKELIARLEQDLstiqsiqrpdaegasEQGLEKI 469
Cdd:PLN02939 298 ----WWEKVENLQ----------------------DLLDRATNQVEKAALVLDQNQDL---------------RDKVDKL 336
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110815859 470 PEPIKEATALFYGPSMsssgtlpegqVDSLLSIISSQRERFRTRNQELEAESRMAQHTIQALQSELDSLRADNIK 544
Cdd:PLN02939 337 EASLKEANVSKFSSYK----------VELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLSKLKEESKK 401
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
126-493 |
6.33e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 39.84 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 126 NQKLRETleeynkEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDF------AEKERKLQETQMSTTS 199
Cdd:PLN03229 420 NMKKREA------VKTPVRELEGEVEKLKEQILKAKESSSKPSELALNEMIEKLKKEIdleyteAVIAMGLQERLENLRE 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 200 KLEEAEHKLQTLQTALektrtelfdlktkydeettakADEIEMIMTDLERANQRAevaqreaetlrEQLSSANHSLQLAS 279
Cdd:PLN03229 494 EFSKANSQDQLMHPVL---------------------MEKIEKLKDEFNKRLSRA-----------PNYLSLKYKLDMLN 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 280 QIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLeqqlnakNSTLKQLEEKLKGQAD 359
Cdd:PLN03229 542 EFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEIKEKMEALKAEVASSGASSGDEL-------DDDLKEKVEKMKKEIE 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 360 YE--EVKK----ELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLqsENAtlrISNSDLSGRCAELQIHLTEATAKA 433
Cdd:PLN03229 615 LElaGVLKsmglEVIGVTKKNKDTAEQTPPPNLQEKIESLNEEINKKI--ERV---IRSSDLKSKIELLKLEVAKASKTP 689
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110815859 434 -VEQKELIARLEQDlstiqsIQRPDAEGASEQGLEKIPEPIKEATALFYGPSMSSSGTLPE 493
Cdd:PLN03229 690 dVTEKEKIEALEQQ------IKQKIAEALNSSELKEKFEELEAELAAARETAAESNGSLKN 744
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
142-310 |
6.47e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.18 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 142 EVKNQEVTIKALKEKIREYEQTLksqaetiALEKEQKLQndfaekerkLQETQMSTTSKLEEAEH---KLQTLQTALEKT 218
Cdd:PRK09039 47 EISGKDSALDRLNSQIAELADLL-------SLERQGNQD---------LQDSVANLRASLSAAEAersRLQALLAELAGA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 219 RTELfdlkTKYDEETTAKADEIEMIMtdlERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRsSLE 298
Cdd:PRK09039 111 GAAA----EGRAGELAQELDSEKQVS---ARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGR-RLN 182
|
170
....*....|..
gi 110815859 299 VELAAKEREIAQ 310
Cdd:PRK09039 183 VALAQRVQELNR 194
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
221-371 |
6.82e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.45 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 221 ELFD-LKTKYDEETTAKADEIEMIMTDLERANQRAEV--AQREAETLREQLSSANHSLQlasQIQKAPDVAIEVLTRSSL 297
Cdd:pfam06160 45 EKFEeWRKKWDDIVTKSLPDIEELLFEAEELNDKYRFkkAKKALDEIEELLDDIEEDIK---QILEELDELLESEEKNRE 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110815859 298 EVElaakereiaQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEkLKGQADYEEVKKELNTLK 371
Cdd:pfam06160 122 EVE---------ELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEE-LTESGDYLEAREVLEKLE 185
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
204-372 |
7.37e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 204 AEHKLQTLQTALEKTRTELFDLKTKYDeettAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQL------ 277
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELD----ALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreelg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 278 ----ASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEK 353
Cdd:COG3883 90 erarALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180
....*....|....*....|
gi 110815859 354 LKG-QADYEEVKKELNTLKS 372
Cdd:COG3883 170 KAElEAQQAEQEALLAQLSA 189
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
235-359 |
8.11e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 39.06 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 235 AKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQkapdvaievlTRSSLEVELAAKEREIAQLved 314
Cdd:COG3524 174 AREDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQ----------LIATLEGQLAELEAELAAL--- 240
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 110815859 315 vqrlqasLTKLRENSAsQISQLEQQLNAKNSTLKQLEEKLKGQAD 359
Cdd:COG3524 241 -------RSYLSPNSP-QVRQLRRRIAALEKQIAAERARLTGASG 277
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
33-374 |
8.30e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 33 NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAflTVYKRLIDVPDPVPALDVGQQL 112
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKA--EEARKAEDAKRVEIARKAEDAR 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 113 EIKVQRLHDIETENQKLRETLE----EYNKEFAEVKNQEVTIKALK----EKIREYEQTLKSQAETIALEKEQKLQN-DF 183
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARKAEEvrkaEELRKAEDARKAEAARKAEEerkaEEARKAEDAKKAEAVKKAEEAKKDAEEaKK 1244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 184 AEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQ--RAEVAQREA 261
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakKADEAKKKA 1324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 262 ETLREQlssANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLN 341
Cdd:PTZ00121 1325 EEAKKK---ADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAE 1401
|
330 340 350
....*....|....*....|....*....|...
gi 110815859 342 AKNSTLKQLEEKLKGQADYEEVKKELNTLKSME 374
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKKADEAKKKAEEKKKAD 1434
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
164-366 |
9.48e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 164 LKSQAETIALEKEQKlqndfAEKerklqetqmsttsKLEEAEHKLQTL-QTALEKTRTELFDLKTKYDEETTAKADEIEm 242
Cdd:PRK12704 25 RKKIAEAKIKEAEEE-----AKR-------------ILEEAKKEAEAIkKEALLEAKEEIHKLRNEFEKELRERRNELQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110815859 243 imtDLERANQraevaQREaETLREQLSSANHSlqlasqiqkapdvaievltrsslEVELAAKEREIAQLVEDVQRLQASL 322
Cdd:PRK12704 86 ---KLEKRLL-----QKE-ENLDRKLELLEKR-----------------------EEELEKKEKELEQKQQELEKKEEEL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 110815859 323 TKLREnsaSQISQLEQQLN-----AKNSTLKQLEEKLKGQA-----DYEEVKKE 366
Cdd:PRK12704 134 EELIE---EQLQELERISGltaeeAKEILLEKVEEEARHEAavlikEIEEEAKE 184
|
|
| |
