|
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 |
6.23e-67 |
|
CASP C terminal; This domain is the C-terminal region of the CASP family of proteins. It is a Golgi membrane protein which is thought to have a role in vesicle transport.
Pssm-ID: 462392 [Multi-domain] Cd Length: 247 Bit Score: 219.85 E-value: 6.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 421 ELQVRITEAVATATEQRELIARLEQDLSIIQSIQR--PDAEGAAEHRLEKIPEPIKEATAlfyGPAA-----PASGALPE 493
Cdd:pfam08172 1 TLQEELSSLNAELEEQQELNAKLENDLLKVQDEASnaFSFNDASSAGSGVSRYPPSGGRR---SPTSsiisgFEPSESSS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 494 GQVDSLLSIISSQRERFRARNQELEAENRLAQHTLQALQSELDSLRADNIKLFEKIKFLQSYPGRGSGSDDTEL------ 567
Cdd:pfam08172 78 SSDSSILPIVTSQRDRFRQRNAELEEELRKQFETISSLRQEIASLQKDNLKLYEKTRYLQSYNRGGGGGTKSSSstsssa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 568 ----------------RYSSQYEERLDPFSSFSKRERQRKYLSLSPWDKATLSMGRLVLSNKMARTIGFFYTLFLHCLVF 631
Cdd:pfam08172 158 saygnnpnpsdvealdKYRKAYEESLNPFAAFRGRESERAYKRLSPLERLVLSLTRLVLANRTSRNLFFFYCLALHLLVF 237
|
250
....*....|
gi 31652238 632 LVLYKLAWSE 641
Cdd:pfam08172 238 FTLYYVSNSS 247
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
18-540 |
2.08e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 18 QQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTpedlrkqvaplLKSFQGEIDALSKRSKEAEAAFLNVYKRLi 97
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAE-----------LEELEAELAELEAELEELRLELEELELEL- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 98 dvpdpvpaLDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQ 177
Cdd:COG1196 284 --------EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 178 kLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVA 257
Cdd:COG1196 356 -AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 258 QREAETLREQLSSANHSLQLASQIQKapdvaievltrssLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQIsQLE 337
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEA-------------LLELLAELLEEAALLEAALAELLEELAEAAARLLLLL-EAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 338 QQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAG---------TQDAAKPLEVLLLEKNRSLQSENAAL 408
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAaalqnivveDDEVAAAAIEYLKAAKAGRATFLPLD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 409 RISNSDLSGRCAELQVRITEAVATATEQRELIARLEQDLSIIQSIQR-PDAEGAAEHRLEKIPEPIKEATAlfYGPAAPA 487
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLvAARLEAALRRAVTLAGRLREVTL--EGEGGSA 658
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 31652238 488 SGALPEGQVDSLLSIISSQRERFRARNQELEAENRLAQHTLQALQSELDSLRA 540
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-375 |
7.25e-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: 68.93 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 107 DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIA--LEKEQKLQNDFA 184
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEerIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 185 EKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQRA 254
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 255 EVAQREAETLREQLSSANHSLqlaSQIQKAPDVAIEVLTrsSLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQIS 334
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEI---EELEELIEELESELE--ALLNERASLEEALALLRSELEELSEELRELES----KRS 911
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 31652238 335 QLEQQLSAKNSTLKQLEEKLKG-QADYEEVKKELNILKSMEF 375
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGlEVRIDNLQERLSEEYSLTL 953
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
16-541 |
8.52e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 8.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTpEDLRKQVAPLLKSfQGEIDALSKRSKEAEAAFLNVYKR 95
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-AEEYELLAELARL-EQDIARLEERRRELEERLEELEEE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 96 LidvpdpvpaLDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEK 175
Cdd:COG1196 325 L---------AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 176 EQKLQNdfAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAE 255
Cdd:COG1196 396 AELAAQ--LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 256 VAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDV------------QRLQASLT 323
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEaayeaaleaalaAALQNIVV 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 324 KLRENSASQISQLEQQLSAKNSTLkqLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQS 403
Cdd:COG1196 554 EDDEVAAAAIEYLKAAKAGRATFL--PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAAR 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 404 ENAALRISNS------DLSGRCAELQVRITEAVATATEQRELIARLEQDLSIIQSIQRPDAEGAAEHRLEKIPEPIKEAT 477
Cdd:COG1196 632 LEAALRRAVTlagrlrEVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAE 711
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31652238 478 ALFYGPAAPASGALPEGQVDSLLSIISSQRERFRARNQELEAENRLAQHTLQALQSELDSLRAD 541
Cdd:COG1196 712 AEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
105-332 |
2.28e-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: 56.70 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 105 ALDLGQQLQLKVQRLH-DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIAL--EKEQKLQN 181
Cdd:COG4942 18 QADAAAEAEAELEQLQqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEleKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 182 DFAEKERKLQET-----QMSTTSKLEEAEHKVQSLQTAlekTRTELFDLKTKYDEEttaKADEIEMIMTDLERANQRAEV 256
Cdd:COG4942 98 ELEAQKEELAELlralyRLGRQPPLALLLSPEDFLDAV---RRLQYLKYLAPARRE---QAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31652238 257 AQREAETLREQLSSANHSLQLASQIQKApdvaievlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 332
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQK--------LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
117-455 |
4.10e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 117 QRLHDIETENQKLRETLE---EYNKEFAEVKNQE------VTIKALKEKIREYEQTLknqaetialEKEQKLQNDFAEKE 187
Cdd:TIGR02168 189 DRLEDILNELERQLKSLErqaEKAERYKELKAELrelelaLLVLRLEELREELEELQ---------EELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 188 RKLQETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTkydeettakadEIEMIMTDLERANQRAEVAQREAETLREQ 267
Cdd:TIGR02168 260 AELQELE----EKLEELRLEVSELEEEIEELQKELYALAN-----------EISRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 268 LSSANHSLQLASQIQKAPDVAIEVLTRSSleVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTL 347
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEEL--ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 348 KQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEknrsLQSENAALRISNSDLSGRCAELQVRIT 427
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE----LQEELERLEEALEELREELEEAEQALD 478
|
330 340
....*....|....*....|....*...
gi 31652238 428 EAVATATEQRELIARLEQDLSIIQSIQR 455
Cdd:TIGR02168 479 AAERELAQLQARLDSLERLQENLEGFSE 506
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
58-355 |
4.37e-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: 56.24 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 58 EDLRKQVAPLL---KSFQGEIDALSKRSKEAEAaflnvykrlIDVPDPVPA---LDLGQQLQLKVQRLHDIETENQKLRE 131
Cdd:pfam05622 17 HELDQQVSLLQeekNSLQQENKKLQERLDQLES---------GDDSGTPGGkkyLLLQKQLEQLQEENFRLETARDDYRI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 132 TLEEYNKEFAE--VKNQEVT-----IKALKEKIREYEQTLK--NQAETIALEKEQKLQ--NDFAEKERKLQETQ---MST 197
Cdd:pfam05622 88 KCEELEKEVLElqHRNEELTslaeeAQALKDEMDILRESSDkvKKLEATVETYKKKLEdlGDLRRQVKLLEERNaeyMQR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 198 TSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLEranQRAEVAQREAETL---REQLSSANHS 274
Cdd:pfam05622 168 TLQLEEELKKANALRGQLETYKRQVQELHGKLSEESK-KADKLEFEYKKLE---EKLEALQKEKERLiieRDTLRETNEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 275 LQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE----NSASQISQLEQQLSAKNSTLKQL 350
Cdd:pfam05622 244 LRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLgqegSYRERLTELQQLLEDANRRKNEL 323
|
....*
gi 31652238 351 EEKLK 355
Cdd:pfam05622 324 ETQNR 328
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
82-406 |
1.00e-07 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 55.35 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 82 SKEAEAAFLNVYKRLIDVPDPVPALdlgQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT-----IKALKEK 156
Cdd:COG5185 221 LLEKAKEIINIEEALKGFQDPESEL---EDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANnlikqFENTKEK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 157 IREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYD-EETTA 235
Cdd:COG5185 298 IAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 236 KAD-----------EIEMIMTDLERANQRAE--------VAQREAETLREQLSSANHSLQLASQIQKA-------PDVAI 289
Cdd:COG5185 378 ELDsfkdtiestkeSLDEIPQNQRGYAQEILatledtlkAADRQIEELQRQIEQATSSNEEVSKLLNEliselnkVMREA 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 290 EVLTRSSLEVELAAKEREIAQ----LVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEvkk 365
Cdd:COG5185 458 DEESQSRLEEAYDEINRSVRSkkedLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARG--- 534
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 31652238 366 ELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENA 406
Cdd:COG5185 535 YAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQ 575
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
127-351 |
2.88e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.15 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 127 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALekEQKLQNDFAEKERKLQETQM-STTSKLEEAE 205
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELeELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 206 HKVQSLQTALEKTRTELFDLKTKYDEettAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQiqkap 285
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRG---NGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE----- 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31652238 286 dvaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLE 351
Cdd:COG4913 381 --------------EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
117-452 |
4.86e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 117 QRLHDIETENQKLRETLEEYNKEfaevKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQms 196
Cdd:TIGR02169 184 ENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLT-- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 197 ttsklEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQ 276
Cdd:TIGR02169 258 -----EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA------K 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 277 LASQIQKApdvaieVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRensaSQISQLEQQLSAKNSTLKQLEEKLkg 356
Cdd:TIGR02169 327 LEAEIDKL------LAEIEELEREIEEERKRRDKLTEEYAELKEELEDLR----AELEEVDKEFAETRDELKDYREKL-- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 357 qadyEEVKKELNILKsmefapsegaGTQDAakplevlLLEKNRSLQSENAALRISNSDLSGRCAELQVRITEAVATATEQ 436
Cdd:TIGR02169 395 ----EKLKREINELK----------RELDR-------LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
|
330
....*....|....*.
gi 31652238 437 RELIARLEQDLSIIQS 452
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQ 469
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
67-373 |
4.49e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 4.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 67 LLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVpdpvpalDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ 146
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELREL-------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAE 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 147 EvtIKALKEKIREYEQTLKNQAETiaLEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQ-TALEKTRTELFDL 225
Cdd:PRK03918 526 E--YEKLKEKLIKLKGEIKSLKKE--LEKLEELKKKLAELEKKLDELE----EELAELLKELEELGfESVEELEERLKEL 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 226 KTKYDEETTAKADEIEmimtdLERANQRAEVAQREAETLREQLSSANHSLQLASQiqkapdvAIEVLTRSSLEVELAAKE 305
Cdd:PRK03918 598 EPFYNEYLELKDAEKE-----LEREEKELKKLEEELDKAFEELAETEKRLEELRK-------ELEELEKKYSEEEYEELR 665
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31652238 306 REIAQLVEDVQRLQAsltklrensasQISQLEQQLSAKNSTLKQLEEKLKgqaDYEEVKKELNILKSM 373
Cdd:PRK03918 666 EEYLELSRELAGLRA-----------ELEELEKRREEIKKTLEKLKEELE---EREKAKKELEKLEKA 719
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
110-270 |
5.56e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 110 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERK 189
Cdd:COG4913 274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 190 LQETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 269
Cdd:COG4913 354 LEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
.
gi 31652238 270 S 270
Cdd:COG4913 430 S 430
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
110-283 |
6.49e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 110 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERK 189
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAE---LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 190 LQETQMSttskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAK----ADEIEMIMTDLERANQRAEVAQREAETLR 265
Cdd:COG4717 151 LEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEELE 226
|
170
....*....|....*...
gi 31652238 266 EQLSSANHSLQLASQIQK 283
Cdd:COG4717 227 EELEQLENELEAAALEER 244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
141-380 |
7.02e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 7.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 141 AEVKNQEVTIKALKEKIREYEQTLKNQAETI--ALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKT 218
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEkaLLKQLAALERRIAALARRIRALE----QELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 219 RTELFDLKTKYDE-----ETTAKADEIEMIM--TDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAiev 291
Cdd:COG4942 96 RAELEAQKEELAEllralYRLGRQPPLALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE--- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 292 ltRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRensaSQISQLEQQLSAKNSTLKQLEEKLKGQAdyEEVKKELNILK 371
Cdd:COG4942 173 --RAELEALLAELEEERAALEALKAERQKLLARLE----KELAELAAELAELQQEAEELEALIARLE--AEAAAAAERTP 244
|
....*....
gi 31652238 372 SMEFAPSEG 380
Cdd:COG4942 245 AAGFAALKG 253
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
128-408 |
7.45e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 7.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 128 KLRETLEEYNKEFAEVKNQEVTIKALKEKIRE--YEQTLKNQAETIALEKEQKLQNDFAEKERKLQEtqmsttsKLEEAE 205
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE-------RLEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 206 HKVQSLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLER--ANQRAEVAQREAETLREQLSSANHSLQlasqiqk 283
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLR------- 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 284 apdvaievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS----------QISQLEQQLSAKNSTLKQLEEK 353
Cdd:TIGR02169 816 ------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiekeienlngKKEELEEELEELEAALRDLESR 883
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 31652238 354 LKG-QADYEEVKKElniLKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAAL 408
Cdd:TIGR02169 884 LGDlKKERDELEAQ---LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEI 936
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
15-316 |
1.15e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.90 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 15 FDLQQLQRELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAflnv 92
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELesKLDELAEELAELEEKLEELKEELESLEAELEELEAE---- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 93 ykrlidvpdpvpaldlgqqlqlkvqrLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIA 172
Cdd:TIGR02168 367 --------------------------LEELESRLEELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDRRE 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 173 LEKEQKLQNDFAEKERKLQETQMSTTSK---LEEAEHKVQSLQTALEKTRTELFDLKTKYDeETTAKADEIEMIMTDLER 249
Cdd:TIGR02168 418 RLQQEIEELLKKLEEAELKELQAELEELeeeLEELQEELERLEEALEELREELEEAEQALD-AAERELAQLQARLDSLER 496
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31652238 250 ANQRAEVAQREAETLREQLSSANHSLQLASQIqkapdvaIEVLTRSSLEVELAAKEREIAQLVEDVQ 316
Cdd:TIGR02168 497 LQENLEGFSEGVKALLKNQSGLSGILGVLSEL-------ISVDEGYEAAIEAALGGRLQAVVVENLN 556
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
162-475 |
1.29e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 162 QTLKNQAETIALEKEQK-LQNDFAEKERKLQETQmSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEI 240
Cdd:TIGR02168 671 SILERRREIEELEEKIEeLEEKIAELEKALAELR-KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 241 EMIMTDLERANQRAEVAQREAETLREQLSSAN-HSLQLASQIQKAPDvAIEVLTR--SSLEVELAAKEREIAQLVEDVQR 317
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEAEEELAEAEaEIEELEAQIEQLKE-ELKALREalDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 318 LQ---ASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQAdyEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLL 394
Cdd:TIGR02168 829 LErriAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE--SELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 395 LEKNRSLQSENAALRISNSDLSGRCAELQVRITEAVATATEQreliARLEQDLSIIQSIQRPDAEGAAEHRLEKIPEPIK 474
Cdd:TIGR02168 907 ESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE----YSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
|
.
gi 31652238 475 E 475
Cdd:TIGR02168 983 E 983
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
107-372 |
1.48e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 107 DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEfaeVKNQEVTIKALKEKIreyeQTLKNQAETIALEKEQKLQNDF--- 183
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE---LEQNNKKIKELEKQL----NQLKSEISDLNNQKEQDWNKELkse 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 184 -AEKERKLQETQmsttSKLEEAEHKVQSLQ---TALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQraevaqr 259
Cdd:TIGR04523 316 lKNQEKKLEEIQ----NQISQNNKIISQLNeqiSQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ------- 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 260 EAETLREQLSSANHSLQLASQIQKAPDVAIEVltrssLEVELAAKEREIAQLVEDvqrlqasltklRENSASQISQLEQQ 339
Cdd:TIGR04523 385 EIKNLESQINDLESKIQNQEKLNQQKDEQIKK-----LQQEKELLEKEIERLKET-----------IIKNNSEIKDLTNQ 448
|
250 260 270
....*....|....*....|....*....|....
gi 31652238 340 LSAKNSTLKQLEEKLKGQADY-EEVKKELNILKS 372
Cdd:TIGR04523 449 DSVKELIIKNLDNTRESLETQlKVLSRSINKIKQ 482
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
117-445 |
1.73e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 117 QRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKEQKLQNDFAEKERKLQETQMS 196
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLV--QTALRQQEKIERYQADLEELEERLEEQNEV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 197 T---TSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERANQ--------------RAEVAQR 259
Cdd:PRK04863 371 VeeaDEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQT-RAIQYQQAVQALERAKQlcglpdltadnaedWLEEFQA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 260 EAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVelaakEREIAQlvedvQRLQASLTKLRE--NSASQISQLE 337
Cdd:PRK04863 450 KEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEV-----SRSEAW-----DVARELLRRLREqrHLAEQLQQLR 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 338 QQLSAknstlkqLEEKLKGQADYEEVKKELNilKSMEFAPSEGAGTQDAAKPLEVLLLeknrSLQSENAALRISNSDLSG 417
Cdd:PRK04863 520 MRLSE-------LEQRLRQQQRAERLLAEFC--KRLGKNLDDEDELEQLQEELEARLE----SLSESVSEARERRMALRQ 586
|
330 340
....*....|....*....|....*...
gi 31652238 418 RCAELQVRITEAVATATEQRELIARLEQ 445
Cdd:PRK04863 587 QLEQLQARIQRLAARAPAWLAAQDALAR 614
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
233-466 |
1.90e-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: 47.45 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 233 TTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQiqkapdvAIEVLTR--SSLEVELAAKEREIAQ 310
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-------RIAALARriRALEQELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 311 LVEDVQRLQASLTKLRENSASQISQLEQQ---------LSAKNST--------LKQLEEKLKGQAD-YEEVKKELNILKS 372
Cdd:COG4942 88 LEKEIAELRAELEAQKEELAELLRALYRLgrqpplallLSPEDFLdavrrlqyLKYLAPARREQAEeLRADLAELAALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 373 mefapsEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSGRCAELQVRITEAVATATEQRELIARLEQDLSIIQS 452
Cdd:COG4942 168 ------ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
250
....*....|....
gi 31652238 453 IQRPDAEGAAEHRL 466
Cdd:COG4942 242 RTPAAGFAALKGKL 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
232-452 |
2.23e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 232 ETTAKADEIEMIMTDLERANQRAEVAQREAETLR------EQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKE 305
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 306 REIAQLVEDVQRLQASLTKLRE-----------NSASQISQLEQQLSAKNSTLKQLEEKLkgqADYEEVKKELnilksme 374
Cdd:COG4913 302 AELARLEAELERLEARLDALREeldeleaqirgNGGDRLEQLEREIERLERELEERERRR---ARLEALLAAL------- 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31652238 375 fapseGAGTQDAAKPLEVLLLEKNRSLQSENAALrisnsdlsgrcAELQVRITEAVATATEQRELIARLEQDLSIIQS 452
Cdd:COG4913 372 -----GLPLPASAEEFAALRAEAAALLEALEEEL-----------EALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
151-353 |
2.72e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 47.32 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 151 KALKEKIREYEQTLKNQAETIALEKEQ-KLQNDFAEKERKL-----QETQMSTTSKLEEAE-HKVQSLQT---------- 213
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKngeniARKQNKYDELVEEAKtIKAEIEELtdellnlvmd 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 214 ------ALEKTRTELFDLKTKYD-----EETTAKADEIEMIMTDLERANQRaevaqreAETLREQLSSANHSL-QLASQI 281
Cdd:PHA02562 250 iedpsaALNKLNTAAAKIKSKIEqfqkvIKMYEKGGVCPTCTQQISEGPDR-------ITKIKDKLKELQHSLeKLDTAI 322
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31652238 282 QKAPDVAIEVLTRSS----LEVELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLSAKNSTLKQLEEK 353
Cdd:PHA02562 323 DELEEIMDEFNEQSKklleLKNKISTNKQSLITLVDKAKKVKAAIEELqaeFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
123-539 |
4.00e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.96 E-value: 4.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 123 ETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIAlekeqklqndfaEKERKLQETQmsttsKLE 202
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEE---IERYEEQREQARETRDEADEVLE------------EHEERREELE-----TLE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 203 EAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQ 282
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 283 KAPDVAIEVLTRSSLEVELAAKE-REIAQLVEDvqRLQASLTKLREnSASQISQLEQQLSAKNSTLKQLEEKLKGQADY- 360
Cdd:PRK02224 338 QAHNEEAESLREDADDLEERAEElREEAAELES--ELEEAREAVED-RREEIEELEEEIEELRERFGDAPVDLGNAEDFl 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 361 EEVKKELNILKSMEfapsegagtqdaaKPLEVLL------LEKNRSLQSEnaalrisnsdlsGRCAEL--QVRITEAVAT 432
Cdd:PRK02224 415 EELREERDELRERE-------------AELEATLrtarerVEEAEALLEA------------GKCPECgqPVEGSPHVET 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 433 ATEQRELIARLEQDLSIIQS--------IQRPDAEGAAEHRLEKIPEPIKEATALfygpaapasgalpegqVDSLLSIIS 504
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEeveeveerLERAEDLVEAEDRIERLEERREDLEEL----------------IAERRETIE 533
|
410 420 430
....*....|....*....|....*....|....*...
gi 31652238 505 SQRER---FRARNQELEAENRLAQHTLQALQSELDSLR 539
Cdd:PRK02224 534 EKRERaeeLRERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
119-414 |
4.56e-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: 46.97 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 119 LHDIETENQKLRETLEEYNKEFAevKNQEVTI--------KALKEKIREYEQTLKNqAETIALEKEQKLQNDFAEKERKL 190
Cdd:TIGR01612 988 LNDYEAKNNELIKYFNDLKANLG--KNKENMLyhqfdekeKATNDIEQKIEDANKN-IPNIEIAIHTSIYNIIDEIEKEI 1064
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 191 -QETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKydEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQls 269
Cdd:TIGR01612 1065 gKNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGK--EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKK-- 1140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 270 SANHSLQLASQIQKAPDVAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLEQQLSA----KNS 345
Cdd:TIGR01612 1141 SENYIDEIKAQINDLEDVADKAISNDDPE-EIEKKIENIVTKIDKKKNIYDEIKKL----LNEIAEIEKDKTSleevKGI 1215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31652238 346 TL---KQLEEKLKGQADyEEVKKELNILKSMEfAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSD 414
Cdd:TIGR01612 1216 NLsygKNLGKLFLEKID-EEKKKSEHMIKAME-AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDD 1285
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
187-373 |
9.59e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 187 ERKLQETQMSTT---SKLEEAEHKVQSLQTALE--KTRTELFDLktkyDEETTAKADEIEMIMTDLERANQRAEVAQREA 261
Cdd:COG3206 167 ELRREEARKALEfleEQLPELRKELEEAEAALEefRQKNGLVDL----SEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 262 ETLREQLSSanhSLQLASQIQKAPDVAIEVLTRSSLEVELA--------------AKEREIA----QLVEDVQRLQASLT 323
Cdd:COG3206 243 AALRAQLGS---GPDALPELLQSPVIQQLRAQLAELEAELAelsarytpnhpdviALRAQIAalraQLQQEAQRILASLE 319
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 31652238 324 KLRENSASQISQLEQQLSAKNSTLKQLEEKlkgQADYEEVKKELNILKSM 373
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPEL---EAELRRLEREVEVAREL 366
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
301-578 |
1.14e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 301 LAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLSAknstLKQLEEKLKGQADYEEVKKELnilksmefapseg 380
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEA----ELDALQERREA----LQRLAEYSWDEIDVASAEREI------------- 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 381 agtqdaakplevllleknRSLQSENAALRISNSDLsgrcAELQVRITEAVATATEQRELIARLEQDlsiiqsiqrpdaEG 460
Cdd:COG4913 671 ------------------AELEAELERLDASSDDL----AALEEQLEELEAELEELEEELDELKGE------------IG 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 461 AAEHRLEKIPEPIKEATALFYGPAAPASGALpegqvdsllsiissqRERFRARNQELEAENRLAQHtLQALQSELDSLRA 540
Cdd:COG4913 717 RLEKELEQAEEELDELQDRLEAAEDLARLEL---------------RALLEERFAAALGDAVEREL-RENLEERIDALRA 780
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 31652238 541 DNIKLFEKI-----KFLQSYPGRGSGSdDTELRYSSQYEERLD 578
Cdd:COG4913 781 RLNRAEEELeramrAFNREWPAETADL-DADLESLPEYLALLD 822
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
16-288 |
1.55e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 16 DLQQLQRELDAtatvLANRQDESEQSRKRLIEQsrefkkntpedlrkqvaplLKSFQGEIDALSKRSKEAEaaflnvykr 95
Cdd:COG4942 28 ELEQLQQEIAE----LEKELAALKKEEKALLKQ-------------------LAALERRIAALARRIRALE--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 96 lidvpdpvpaldlgQQLQLKVQRLHDIETENQKLRETLEEYNKEFAevknqEVTIKALKEKIREYEQTLKNQAETIALEK 175
Cdd:COG4942 76 --------------QELAALEAELAELEKEIAELRAELEAQKEELA-----ELLRALYRLGRQPPLALLLSPEDFLDAVR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 176 EQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAE 255
Cdd:COG4942 137 RLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216
|
250 260 270
....*....|....*....|....*....|...
gi 31652238 256 VAQREAETLREQLSSANHSLQLASQIQKAPDVA 288
Cdd:COG4942 217 ELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
117-371 |
1.67e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 117 QRLHDIETENQKLRETLEEYNKEFAEvKNQEvtIKALKEKIREYEQTLKNQAETIA--LEKEQKLQNDFAEKERKLQETQ 194
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKS-KEKE--LKKLNEEKKELEEKVKDLTKKISslKEKIEKLESEKKEKESKISDLE 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 195 -----MSTTSKLEEAEHKVQSLQ----------TALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQR 259
Cdd:TIGR04523 545 delnkDDFELKKENLEKEIDEKNkeieelkqtqKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKK 624
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 260 EAETLREQ----LSSANHSLQLASQIQKAPDVAIEVLTrsslevELAAKEREIAQLVEDVqrLQASLTKLRENSASQISQ 335
Cdd:TIGR04523 625 ENEKLSSIikniKSKKNKLKQEVKQIKETIKEIRNKWP------EIIKKIKESKTKIDDI--IELMKDWLKELSLHYKKY 696
|
250 260 270
....*....|....*....|....*....|....*.
gi 31652238 336 LEQQLsaKNSTLKQLEEKlkgqadYEEVKKELNILK 371
Cdd:TIGR04523 697 ITRMI--RIKDLPKLEEK------YKEIEKELKKLD 724
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
196-389 |
1.74e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 196 STTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL 275
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 276 QLASQIQKAPDV---------------AIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQ 338
Cdd:COG3883 96 YRSGGSVSYLDVllgsesfsdfldrlsALSKIADADADLleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 31652238 339 QLSAKNSTLKQLEEKlkgQADYEEVKKELNILKSMEFAPSEGAGTQDAAKP 389
Cdd:COG3883 176 QQAEQEALLAQLSAE---EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
25-358 |
1.78e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 25 DATATVLANRQDE----SEQSRKRLIEQ--SREFKKNTPEDLRKQVAPLlksfQGEIDALSKRSKEAEAAFLNVYKRLID 98
Cdd:PRK02224 306 DADAEAVEARREEledrDEELRDRLEECrvAAQAHNEEAESLREDADDL----EERAEELREEAAELESELEEAREAVED 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 99 VPDPVPALDlgQQLQLKVQRLHDIETEnqklRETLEEYNKEFAEVKNqevtikALKEKIREYEQTLKNQAETIALEKEQK 178
Cdd:PRK02224 382 RREEIEELE--EEIEELRERFGDAPVD----LGNAEDFLEELREERD------ELREREAELEATLRTARERVEEAEALL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 179 LQNDFAEKERKLQETQMSTTskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAK--ADEIEMIMTDLERANQRAEV 256
Cdd:PRK02224 450 EAGKCPECGQPVEGSPHVET--IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaEDRIERLEERREDLEELIAE 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 257 AQREAETLREQLSSANHSLQ-LASQIQKAPDVAIEVLTRS-SLEVELAAKEREIAQLVEDVQRLQ--ASLTKLRENSASQ 332
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAeLEAEAEEKREAAAEAEEEAeEAREEVAELNSKLAELKERIESLEriRTLLAAIADAEDE 607
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 31652238 333 ISQLEQQ--------------LSAKNSTLKQLEEKLKGQA 358
Cdd:PRK02224 608 IERLREKrealaelnderrerLAEKRERKRELEAEFDEAR 647
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
115-453 |
1.81e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.73 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 115 KVQRLHDIETENQKLRETLEEYNKEFaevKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQ 194
Cdd:pfam17380 235 KMERRKESFNLAEDVTTMTPEYTVRY---NGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKARE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 195 MSTTSKLEEAEHKVQSL------------QTALEKTRT-ELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA 261
Cdd:pfam17380 312 VERRRKLEEAEKARQAEmdrqaaiyaeqeRMAMERERElERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 262 ETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVElAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLS 341
Cdd:pfam17380 392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE-EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 342 AKNSTLKQLEEKLKGQADYEEVKKELnILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSGRCAE 421
Cdd:pfam17380 471 ERKRKKLELEKEKRDRKRAEEQRRKI-LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEME 549
|
330 340 350
....*....|....*....|....*....|..
gi 31652238 422 LQVRITEAVATATEQRELIARLEQDLSIIQSI 453
Cdd:pfam17380 550 ERRRIQEQMRKATEERSRLEAMEREREMMRQI 581
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
117-317 |
1.90e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 117 QRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQklqndfAEKERKLQETQmS 196
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREI------AELEAELERLD-A 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 197 TTSKLEEAEHKVQSLQTALEKTRTELFDLKTKY---DEETTAKADEIEMIMTDLERANQRAEVAQRE-AETLREQLSSAN 272
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDA 762
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 31652238 273 HSLQLASQIQKApdvaievltRSSLEVELAAKEREIAQLVEDVQR 317
Cdd:COG4913 763 VERELRENLEER---------IDALRARLNRAEEELERAMRAFNR 798
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
106-325 |
2.00e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 106 LDLGQQlQLKVQRLHdIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKNQAETIalekeQKLQN 181
Cdd:PHA02562 190 IDHIQQ-QIKTYNKN-IEEQRKKNGENIARKQNKYDELVEEAKTIKAeieeLTDELLNLVMDIEDPSAAL-----NKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 182 DFAEKERKLQ----ETQMST--------TSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakadeiemimtdlER 249
Cdd:PHA02562 263 AAAKIKSKIEqfqkVIKMYEkggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE--------------EI 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31652238 250 ANQRAEvAQREAETLREQLSSANHSLQLASQIQKAPDVAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL 325
Cdd:PHA02562 329 MDEFNE-QSKKLLELKNKISTNKQSLITLVDKAKKVKAAIE-----ELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
11-301 |
2.02e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.68 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 11 YWKRFDLQQLQRELDATaTVLANRQDESEQSRKRLIE---QSREFK--KNTPEDLRKQVAPLLKSFQGEIDALSKrSKEA 85
Cdd:COG5022 851 FGRSLKAKKRFSLLKKE-TIYLQSAQRVELAERQLQElkiDVKSISslKLVNLELESEIIELKKSLSSDLIENLE-FKTE 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 86 EAAFLnvyKRLIDVPDPVPALDLGQQLQLKVQRLHdieTENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLK 165
Cdd:COG5022 929 LIARL---KKLLNNIDLEEGPSIEYVKLPELNKLH---EVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELA 1002
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 166 N--------QAETIALEKEQK----LQNDF-------AEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLK 226
Cdd:COG5022 1003 ElskqygalQESTKQLKELPVevaeLQSASkiissesTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQ 1082
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31652238 227 TKYDEETTAKADEIEmiMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQI-QKAPDVAIEVLTRSSLEVEL 301
Cdd:COG5022 1083 LYQLESTENLLKTIN--VKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLsQLVNTLEPVFQKLSVLQLEL 1156
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
56-356 |
2.36e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 56 TPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDpvpaldlgQQLQLKVQRLHDIETENQKLRETLEE 135
Cdd:pfam12128 615 SAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD--------EKQSEKDKKNKALAERKDSANERLNS 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 136 YNKEfaevknqevtIKALKEKIREYEQTLKNQAETIALEKEQKLQNdfAEKERKLQETQMSTTSKLEEAEHKVQslQTAL 215
Cdd:pfam12128 687 LEAQ----------LKQLDKKHQAWLEEQKEQKREARTEKQAYWQV--VEGALDAQLALLKAAIAARRSGAKAE--LKAL 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 216 EKTRTElfDLKTK-YDEETTAK-ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQlasqiqkapdvaievlt 293
Cdd:pfam12128 753 ETWYKR--DLASLgVDPDVIAKlKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLA----------------- 813
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31652238 294 rssleVELAAKEREIAQLVEDVQRLQASlTKLRensasqISQLEQQLSAKNSTLKQLEEKLKG 356
Cdd:pfam12128 814 -----TQLSNIERAISELQQQLARLIAD-TKLR------RAKLEMERKASEKQQVRLSENLRG 864
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
119-371 |
2.45e-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: 44.43 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 119 LHDIETENQKLRETLEEYNK---EFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQM 195
Cdd:pfam10174 201 LDQKEKENIHLREELHRRNQlqpDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVY 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 196 STTSKLeeAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQREAETLREQLSSAN 272
Cdd:pfam10174 281 KSHSKF--MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDckqHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 273 HSLQ---------------LASQIQKAPDV------AIEVLTR--SSLEVELAAKEREIAQLVEDVQRLQASLTklreNS 329
Cdd:pfam10174 359 SFLNkktkqlqdlteekstLAGEIRDLKDMldvkerKINVLQKkiENLQEQLRDKDKQLAGLKERVKSLQTDSS----NT 434
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 31652238 330 ASQISQLEQQLSAKNSTLKQLEEK--LKGQADYEEV---KKELNILK 371
Cdd:pfam10174 435 DTALTTLEEALSEKERIIERLKEQreREDRERLEELeslKKENKDLK 481
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
16-370 |
2.53e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 16 DLQQLQRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEidALSKRSKEAEaaflNVYKR 95
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE--ELEKKAEEYE----KLKEK 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 96 LIDVPdpvpaldlGQQLQLK--VQRLHDIETENQKLRETLEEYNKEFAEVKNQEV-----TIKALKEKIREYEQtlknqa 168
Cdd:PRK03918 534 LIKLK--------GEIKSLKkeLEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELEP------ 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 169 etiALEKEQKLQNDFAEKERKLQEtQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLE 248
Cdd:PRK03918 600 ---FYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE---EYLELS 672
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 249 RANQRAEVAQREAETLREQLSSAnhslqlasqiqkAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLREN 328
Cdd:PRK03918 673 RELAGLRAELEELEKRREEIKKT------------LEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKER 740
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 31652238 329 SASQISQLEQQLSAK-------NSTLKQLEEKLKGQADYEEVKKELNIL 370
Cdd:PRK03918 741 ALSKVGEIASEIFEEltegkysGVRVKAEENKVKLFVVYQGKERPLTFL 789
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
21-366 |
2.83e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 21 QRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDlRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVP 100
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED-KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA 1443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 101 DPVPALDLGQQLQLKVQRLHDIETENQKLRETLE--EYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQK 178
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK 1523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 179 LQN-DFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMImtDLERANQRAEVA 257
Cdd:PTZ00121 1524 ADEaKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA--EEARIEEVMKLY 1601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 258 QREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLE 337
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
330 340
....*....|....*....|....*....
gi 31652238 338 QQLSAKNSTLKQLEEKLKGQADYEEVKKE 366
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
18-216 |
3.91e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 18 QQLQRELDATATVLANRQDESEQSRKRLIEQS---REFKKNT----PEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFL 90
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEaalEEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 91 NVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAET 170
Cdd:COG3206 244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEA 320
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 31652238 171 ---IALEKEQKLQNDFAEKERKLQETQmSTTSKLEEAEHKVQSLQTALE 216
Cdd:COG3206 321 eleALQAREASLQAQLAQLEARLAELP-ELEAELRRLEREVEVARELYE 368
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
58-250 |
4.57e-04 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 42.74 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 58 EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLNVYKRLIDvpdpvpalDLGQQLQLKVQRLHDI-ETENQKL-RETLEE 135
Cdd:cd22656 113 EEAKKTIKALLDDLLKEAKKYQDKAAKVVDK-LTDFENQTE--------KDQTALETLEKALKDLlTDEGGAIaRKEIKD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 136 YNKEFAevKNQEVTIKALKEKIREYEQTLKNQAETIAleKEQKLQNDFaekerKLQETQM-STTSKLEEAEHKVQSLQTA 214
Cdd:cd22656 184 LQKELE--KLNEEYAAKLKAKIDELKALIADDEAKLA--AALRLIADL-----TAADTDLdNLLALIGPAIPALEKLQGA 254
|
170 180 190
....*....|....*....|....*....|....*.
gi 31652238 215 LEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERA 250
Cdd:cd22656 255 WQAIATDLDSLKDLLEDDIS-KIPAAILAKLELEKA 289
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
21-246 |
5.17e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 21 QRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaaflnvykrlidvP 100
Cdd:PTZ00121 1592 ARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE-------------E 1658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 101 DPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKnqAETIALEKEQKLQ 180
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAEEAK 1736
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 31652238 181 NDFAEKERKLQETQmsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD 246
Cdd:PTZ00121 1737 KEAEEDKKKAEEAK-----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
117-250 |
6.28e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 6.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 117 QRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQTL---KNQAETIALEKEQklqnDFAEKERK 189
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELedleKEIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQKEI----ESLKRRIS 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31652238 190 LQETQMS-TTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERA 250
Cdd:COG1579 107 DLEDEILeLMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
126-439 |
6.55e-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: 42.82 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 126 NQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQA-ETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 204
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 205 EHK-VQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLE--RANQRAE--VAQREAETLREQLSSANHSLQlaS 279
Cdd:pfam07111 138 SQReLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkRAGEAKQlaEAQKEAELLRKQLSKTQEELE--A 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 280 QIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQ---------ASLTKLRENSASQISQL-EQQLSAKNSTLKQ 349
Cdd:pfam07111 216 QVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQedradlqatVELLQVRVQSLTHMLALqEEELTRKIQPSDS 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 350 LEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLLEKNRSLQSENAALRISNSDLSGRCAELQVritEA 429
Cdd:pfam07111 296 LEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEV---ER 372
|
330
....*....|
gi 31652238 430 VATATEQREL 439
Cdd:pfam07111 373 MSAKGLQMEL 382
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
66-369 |
7.60e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.98 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 66 PLLKSFQGEIDALSKRsKEAEAAFLNVYKRLIDvpdpvpALDLGQQLQlkvqrlhDIETENQKLRETLEEYNKEFAEVKN 145
Cdd:PRK11281 36 PTEADVQAQLDALNKQ-KLLEAEDKLVQQDLEQ------TLALLDKID-------RQKEETEQLKQQLAQAPAKLRQAQA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 146 QevtIKALKEKIreyEQTLKNQAETIALEKeqkLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKTRTELFdl 225
Cdd:PRK11281 102 E---LEALKDDN---DEETRETLSTLSLRQ---LESRLAQTLDQLQNAQ----NDLAEYNSQLVSLQTQPERAQAALY-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 226 ktkydeettakadeiemimtdlerANQraevaQREAEtLREQLSS--ANHSLQLASQIQKapdvaievltrssLEVELAA 303
Cdd:PRK11281 167 ------------------------ANS-----QRLQQ-IRNLLKGgkVGGKALRPSQRVL-------------LQAEQAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 304 KEREIA---QLVEDVQRLQASLTKLRENSASQISQLEQQL-------SAKNstLKQLEEKLKGQADYEE---------VK 364
Cdd:PRK11281 204 LNAQNDlqrKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLqllqeaiNSKR--LTLSEKTVQEAQSQDEaariqanplVA 281
|
....*
gi 31652238 365 KELNI 369
Cdd:PRK11281 282 QELEI 286
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
17-539 |
8.47e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 8.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 17 LQQLQRELDATATVLANRQDESEQSRKRL------IEQSREFKKNTPEDLRKQVAPLLK---SFQGEIDAL-SKRSKEAE 86
Cdd:pfam15921 119 LQEMQMERDAMADIRRRESQSQEDLRNQLqntvheLEAAKCLKEDMLEDSNTQIEQLRKmmlSHEGVLQEIrSILVDFEE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 87 AAFLNVYKRliDVPDPVPALDLG-------QQLQLKVQ-----------RLHDIETENQKLRETLEEYNKEFAE--VKNQ 146
Cdd:pfam15921 199 ASGKKIYEH--DSMSTMHFRSLGsaiskilRELDTEISylkgrifpvedQLEALKSESQNKIELLLQQHQDRIEqlISEH 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 147 EVTIKALKEKI---REYEQTLKNQAETIalEKEQKLQND-FAEKERKLQETQMSTTSKLEEA----EHKVQSLQTALEKT 218
Cdd:pfam15921 277 EVEITGLTEKAssaRSQANSIQSQLEII--QEQARNQNSmYMRQLSDLESTVSQLRSELREAkrmyEDKIEELEKQLVLA 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 219 RTELFDLKTKYDE---ETTAKADEIEMIMTDLERANQRAEVAQREAETLREQlsSANHSLQLASQIQKAPDVAIEVLTRS 295
Cdd:pfam15921 355 NSELTEARTERDQfsqESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR--DTGNSITIDHLRRELDDRNMEVQRLE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 296 SLEVELAAK-----EREIAQLVEDVQRLQ--ASLTKLRENSASQISQLEQQLSAKNSTLKQ-----------LEEKLKG- 356
Cdd:pfam15921 433 ALLKAMKSEcqgqmERQMAAIQGKNESLEkvSSLTAQLESTKEMLRKVVEELTAKKMTLESsertvsdltasLQEKERAi 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 357 ---QADYEEVKKELNI-LKSMEFAPSEGAGTQDAAKPLEVLLL---EKNRSL-----QSEN------------AALRISN 412
Cdd:pfam15921 513 eatNAEITKLRSRVDLkLQELQHLKNEGDHLRNVQTECEALKLqmaEKDKVIeilrqQIENmtqlvgqhgrtaGAMQVEK 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 413 SDLSGRCAELQVRITEAVATATEQRELIARLEQDLSIIQsIQRPDAEGAAEHRLEKIPEPIKEATALFYGPAAPASgalp 492
Cdd:pfam15921 593 AQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE-LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRN---- 667
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 31652238 493 egQVDSLLSIISSQRERFRARNQELEAENRLAQHTLQALQSELDSLR 539
Cdd:pfam15921 668 --ELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTR 712
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
106-373 |
9.87e-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: 9.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 106 LDLGQQLQLKVQRLHDIETENQKLRETL--EEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQA----ETIA--LEKEQ 177
Cdd:TIGR00618 628 QDVRLHLQQCSQELALKLTALHALQLTLtqERVREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkEMLAqcQTLLR 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 178 KLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRtELFDLKTKYDEETTAKADE----IEMIMTDLERANQR 253
Cdd:TIGR00618 708 ELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELM-HQARTVLKARTEAHFNNNEevtaALQTGAELSHLAAE 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 254 AEVAQREAETLREQLSsanhslQLASQIQKAPDVAIEVLTrssLEVELAAKEREiaqlvedvqrlqASLTKLRENSASQI 333
Cdd:TIGR00618 787 IQFFNRLREEDTHLLK------TLEAEIGQEIPSDEDILN---LQCETLVQEEE------------QFLSRLEEKSATLG 845
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 31652238 334 sQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSM 373
Cdd:TIGR00618 846 -EITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQI 884
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
118-227 |
1.46e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 41.16 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 118 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAET---IALEKEQKLQNDFA---EKERKLQ 191
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELDrakEKLKKLL 217
|
90 100 110
....*....|....*....|....*....|....*.
gi 31652238 192 ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKT 227
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT 253
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
130-408 |
2.35e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 130 RETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETialekEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQ 209
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR-----KKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQ 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 210 SLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQ---------REAETLREQLSSANHSLQLASQ 280
Cdd:TIGR00606 312 RTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQehirardslIQSLATRLELDGFERGPFSERQ 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 281 IQKAPDVAIEVLTR-----SSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLK 355
Cdd:TIGR00606 392 IKNFHTLVIERQEDeaktaAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSD 471
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 31652238 356 G--QADYEEVKKELNILKSMEFAPSEGAGTQDAA-KPLEVLLLEKNRSLQSENAAL 408
Cdd:TIGR00606 472 RilELDQELRKAERELSKAEKNSLTETLKKEVKSlQNEKADLDRKLRKLDQEMEQL 527
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
110-553 |
2.50e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 41.26 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 110 QQLQLKVQRLHDIETENQKLRETLEeynKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQN------DF 183
Cdd:pfam15921 120 QEMQMERDAMADIRRRESQSQEDLR---NQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEirsilvDF 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 184 AEKERK--LQETQMSTT--SKLEEAEHKV-QSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD-LERANQRAEVA 257
Cdd:pfam15921 197 EEASGKkiYEHDSMSTMhfRSLGSAISKIlRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQhQDRIEQLISEH 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 258 QREAETLREQLSSANHSlqlASQIQKAPDVAIEVLTRSSlevelAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLE 337
Cdd:pfam15921 277 EVEITGLTEKASSARSQ---ANSIQSQLEIIQEQARNQN-----SMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 338 QQLSAKNSTLKQ--------------LEEKL-KGQADYEEVKKELNILKSM-EFAPSEGAGTQDAAKPLEVLLLEKNRSL 401
Cdd:pfam15921 349 KQLVLANSELTEarterdqfsqesgnLDDQLqKLLADLHKREKELSLEKEQnKRLWDRDTGNSITIDHLRRELDDRNMEV 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 402 QSENAALRISNSDLSGRCAelqvRITEAVATATEQRELIARLEQDLSIIQSIQRPDAE--GAAEHRLEKIPEPIKEATal 479
Cdd:pfam15921 429 QRLEALLKAMKSECQGQME----RQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEelTAKKMTLESSERTVSDLT-- 502
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31652238 480 fygpaapASGALPEGQVDSLLSIISSQRERFRARNQELEAENRLAQHtLQALQSELDSLRadnIKLFEKIKFLQ 553
Cdd:pfam15921 503 -------ASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDH-LRNVQTECEALK---LQMAEKDKVIE 565
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
125-293 |
2.74e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 125 ENQKLRETLEEynkefaEVKNQEVTIKALKEKIREYEQTLKNQAEtiALEKeqklqndfaeKERKLQETQMSTTSKLEEA 204
Cdd:PRK12704 65 EIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLE--LLEK----------REEELEKKEKELEQKQQEL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 205 EHKVQSLQTALEKTRTELFDLKTKYDEEttAKadeiEMIMTDLErANQRAEVAQ--REAETLREQLSSANHSLQLASQIQ 282
Cdd:PRK12704 127 EKKEEELEELIEEQLQELERISGLTAEE--AK----EILLEKVE-EEARHEAAVliKEIEEEAKEEADKKAKEILAQAIQ 199
|
170
....*....|..
gi 31652238 283 K-APDVAIEVLT 293
Cdd:PRK12704 200 RcAADHVAETTV 211
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
109-352 |
4.13e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 109 GQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIalekeQKLQNDFAEKER 188
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI-----RELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 189 KLQ--ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLRE 266
Cdd:PRK03918 274 EIEelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE-KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 267 QLSSANHSLQLASQIqKAPDVAIEvltrsSLEVELAAKERE-IAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNS 345
Cdd:PRK03918 353 RLEELEERHELYEEA-KAKKEELE-----RLKKRLTGLTPEkLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
|
....*..
gi 31652238 346 TLKQLEE 352
Cdd:PRK03918 427 AIEELKK 433
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
125-388 |
4.62e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 125 ENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIRE----YEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSK 200
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEvmklYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 201 LEEAEHKVQSLQtalektrtelfdlktKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQ 280
Cdd:PTZ00121 1642 EAEEKKKAEELK---------------KAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 281 IQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTL-KQLEEKLKGQAD 359
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIrKEKEAVIEEELD 1786
|
250 260
....*....|....*....|....*....
gi 31652238 360 YEEVKKELNILKSMEFAPSEGAGTQDAAK 388
Cdd:PTZ00121 1787 EEDEKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
113-268 |
4.71e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 113 QLKVQRLhDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKEQKLQNDFAEKERKLQE 192
Cdd:COG1340 75 ELKEERD-ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ--QTEVLSPEEEKELVEKIKELEKELEK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 193 TQMS--TTSKLEEAEHKVQSLQTALEKTR---TELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQ 267
Cdd:COG1340 152 AKKAleKNEKLKELRAELKELRKEAEEIHkkiKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEE 231
|
.
gi 31652238 268 L 268
Cdd:COG1340 232 I 232
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
68-325 |
4.98e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 68 LKSFQGEIDALSKRSKEAEAAfLNVYKRLIDVpdpvpaLDLGQQLQLKVQRLHDIETENQKLRETLEEynkefaevknQE 147
Cdd:COG3206 177 LEFLEEQLPELRKELEEAEAA-LEEFRQKNGL------VDLSEEAKLLLQQLSELESQLAEARAELAE----------AE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 148 VTIKALKEKIREYEQTLKNQAETIALekeQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKTRTELfdlkt 227
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVI---QQLRAQLAELEAELAELS----ARYTPNHPDVIALRAQIAALRAQL----- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 228 kydeettakADEIEMIMTDLEranQRAEVAQREAETLREQLSsanhslQLASQIQKAPdvaievltrsslevelaAKERE 307
Cdd:COG3206 308 ---------QQEAQRILASLE---AELEALQAREASLQAQLA------QLEARLAELP-----------------ELEAE 352
|
250
....*....|....*...
gi 31652238 308 IAQLVEDVQRLQASLTKL 325
Cdd:COG3206 353 LRRLEREVEVARELYESL 370
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
151-446 |
7.54e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 39.57 E-value: 7.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 151 KALKEKIREYEQTLKNQAETIALEK-EQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKY 229
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLqELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 230 DEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSanhslqlasqiqkapDVAIEVLTRSSLEVELAAKEREIA 309
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAK---------------EEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 310 QLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSmefapSEGAGTQDAAKP 389
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK-----LESERLSSAAKL 392
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 31652238 390 LEVLLLEKNRSLQSENAALRISNSDLSGRCAELQVRITEAVATATEQRELIARLEQD 446
Cdd:pfam02463 393 KEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEE 449
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
32-277 |
8.50e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 39.35 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 32 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVpdpvpaldLGQQ 111
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQ--------LSKK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 112 LQ-LKVQRLHDIETENQKLRETLE----------EYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQ 180
Cdd:pfam09731 303 LAeLKKREEKHIERALEKQKEELDklaeelsarlEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLK 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 181 NDFAEKERKLQETQMsttskleeaehkvQSLQTALEKTRtelfDLKTKYDEETTAKADEIEMIMT---DLERANQRAEVA 257
Cdd:pfam09731 383 DVLVEQEIELQREFL-------------QDIKEKVEEER----AGRLLKLNELLANLKGLEKATSshsEVEDENRKAQQL 445
|
250 260
....*....|....*....|
gi 31652238 258 QREAETLREQLSSANHSLQL 277
Cdd:pfam09731 446 WLAVEALRSTLEDGSADSRP 465
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
115-267 |
8.73e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 8.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 115 KVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQ 194
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK 1703
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31652238 195 MSTTSKLEEAE-HKVQSLQTALEKTRTELFDLKTKyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQ 267
Cdd:PTZ00121 1704 AEELKKKEAEEkKKAEELKKAEEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
234-464 |
8.85e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 38.99 E-value: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 234 TAKADEIEmimtdlERANQRAEVAQREAETLREQLSsanhsLQLASQIQKApdvaievltRSSLEVELAAKEREIAQLVE 313
Cdd:PRK12704 30 EAKIKEAE------EEAKRILEEAKKEAEAIKKEAL-----LEAKEEIHKL---------RNEFEKELRERRNELQKLEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31652238 314 DVQRLQASLtklrENSASQISQLEQQLSAKNSTLKQLEEKLKG-QADYEEVKKELniLKSMEfapsEGAG-TQDAAKple 391
Cdd:PRK12704 90 RLLQKEENL----DRKLELLEKREEELEKKEKELEQKQQELEKkEEELEELIEEQ--LQELE----RISGlTAEEAK--- 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31652238 392 VLLLEKNRSLQSENAALRISNSdlsgrcaelqvrITEAVATATEQRELIarleqdlsIIQSIQRPDAEGAAEH 464
Cdd:PRK12704 157 EILLEKVEEEARHEAAVLIKEI------------EEEAKEEADKKAKEI--------LAQAIQRCAADHVAET 209
|
|
| |
