|
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 ... |
512-732 |
1.17e-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: 223.70 E-value: 1.17e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 512 ELQVRVTEAVATATEQRELIARLEQDLSIIQSIQR--PDAEGAAEHRLEKIPEPIKEATAlfyGPAA-----PASGALPE 584
Cdd:pfam08172 1 TLQEELSSLNAELEEQQELNAKLENDLLKVQDEASnaFSFNDASSAGSGVSRYPPSGGRR---SPTSsiisgFEPSESSS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 585 GQVDSLLSIISSQRERFRARNQELEAENRLAQHTLQALQSELDSLRADNIKLFEKIKFLQSYPGRG-------------- 650
Cdd:pfam08172 78 SSDSSILPIVTSQRDRFRQRNAELEEELRKQFETISSLRQEIASLQKDNLKLYEKTRYLQSYNRGGgggtksssstsssa 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 651 --------SSSDDTELRYSSQYEERLDPFSSFSKRERQRKYLSLSPWDKATLSMGRLVLSNKMARTIGFFYTLFLHCLVF 722
Cdd:pfam08172 158 saygnnpnPSDVEALDKYRKAYEESLNPFAAFRGRESERAYKRLSPLERLVLSLTRLVLANRTSRNLFFFYCLALHLLVF 237
|
250
....*....|
gi 1622917398 723 LVLYKLAWSE 732
Cdd:pfam08172 238 FTLYYVSNSS 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
196-500 |
3.88e-11 |
|
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: 67.00 E-value: 3.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 196 DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIA--LEKEQKLQNDFA 273
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEerIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 274 EKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDE----------ETTAKADEIEMIMTDLERANQRA 343
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElraeltllneEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 344 EVAQREAETLREQLSSANHSLqlasqiqkapdveqaievltrSSLEVELAAKEREIAQLVEDVQRLQASLTKLR---ENS 420
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEI---------------------EELEELIEELESELEALLNERASLEEALALLRselEEL 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 421 ASQISQLEQQLSAKNSTLKQLEEKLkGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALR 500
Cdd:TIGR02168 900 SEELRELESKRSELRRELEELREKL-AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
112-632 |
1.41e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 112 ELDATATVLANRQDESEQSRKRLIEQSREFKKNtpedlRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLidvpdp 191
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEER-----LEELEEELAELEEELEELEEELEELEEELEEAEEEL------ 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 192 vpaLDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQND 271
Cdd:COG1196 354 ---EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 272 FAEKERKLQETQmsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEmimtDLERANQRAEVAQREAE 351
Cdd:COG1196 431 AELEEEEEEEEE-----ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE----ELAEAAARLLLLLEAEA 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 352 TLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQL 431
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDK 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 432 SAKNSTLKQLEEKLKGQADYEEVKKELNILKSMEFAPSE-------GAGTQDAAKPLEVLLMEKNRSLQSENAALRISNS 504
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDtllgrtlVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 505 DLSGRCAELQVRVTEAVATATEQRELIARLEQDLSIIQSIQRPDAEGAAEHRLEKIPEPIKEATAlfygpaapasgalpE 584
Cdd:COG1196 662 LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEAL--------------E 727
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1622917398 585 GQVDSLLSIISSQRERFRARNQELEAENRLAQHTLQALQSELDSLRAD 632
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
171-497 |
2.01e-09 |
|
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: 60.74 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 171 SKEAEAAFLNVYKRLIDVPDPVPALdlgQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVT-----IKALKEK 245
Cdd:COG5185 221 LLEKAKEIINIEEALKGFQDPESEL---EDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANnlikqFENTKEK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 246 IREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYD-EETTA 324
Cdd:COG5185 298 IAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVElSKSSE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 325 KAD-----------EIEMIMTDLERANQRAE--------VAQREAETLREQLSSANHSLQLASQIQKA-----PDVEQAI 380
Cdd:COG5185 378 ELDsfkdtiestkeSLDEIPQNQRGYAQEILatledtlkAADRQIEELQRQIEQATSSNEEVSKLLNEliselNKVMREA 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 381 EVLTRSSLEVELAAKEREIAQ----LVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEvkk 456
Cdd:COG5185 458 DEESQSRLEEAYDEINRSVRSkkedLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARG--- 534
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1622917398 457 ELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENA 497
Cdd:COG5185 535 YAHILALENLIPASELIQASNAKTDGQAANLRTAVIDELTQ 575
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
200-668 |
6.54e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 200 QLQLKVQRLHDIETENQKLRETLEEYNKEFAEvknQEVTIKALKEKIREYEQTLKNQAETIalekeQKLQNDFAEKERKL 279
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEE---LEAELAELEAELEELRLELEELELEL-----EEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 280 QEtqmsttskLEEAEHKVQSLQTALEKTRTELfdlktkyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSS 359
Cdd:COG1196 298 AR--------LEQDIARLEERRRELEERLEEL-------EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 360 ANHSLQLASQIQKApdveqaiEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLK 439
Cdd:COG1196 363 AEEALLEAEAELAE-------AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 440 QLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQ---------------DAAKPLEVLL--MEKNRSLQSENAALRIS 502
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEaalleaalaelleelAEAAARLLLLleAEADYEGFLEGVKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 503 NSDLSGRCAELQVRVTEAVATATEQRELIARLEQDlsiIQSIQRPDAEGAAEHRLEKIPEPIKEATALFYGPAAPASGAL 582
Cdd:COG1196 516 LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQN---IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAAL 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 583 PEGQVDSLLSIISSQRERFRARNQELEAENRLAQHTLQALQSELDSLRADNIKLFEKIKFLQSYPGRGSSSDDTELRYSS 662
Cdd:COG1196 593 ARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLA 672
|
....*.
gi 1622917398 663 QYEERL 668
Cdd:COG1196 673 ALLEAE 678
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
194-423 |
1.84e-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: 57.08 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 194 ALDLGQQLQLKVQRLH-DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIAL--EKEQKLQN 270
Cdd:COG4942 18 QADAAAEAEAELEQLQqEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEleKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 271 DFAEKERKLQET-----QMSTTSKLEEAEHKVQSLQTAlekTRTELFDLKTKYDEEttaKADEIEMIMTDLERANQRAEV 345
Cdd:COG4942 98 ELEAQKEELAELlralyRLGRQPPLALLLSPEDFLDAV---RRLQYLKYLAPARRE---QAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917398 346 AQREAETLREQLSSANHSLQLASQIQKApdveqaievlTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 423
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQK----------LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
122-463 |
8.16e-08 |
|
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: 55.80 E-value: 8.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 122 NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQgEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPAL-----D 196
Cdd:TIGR04523 165 KKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLS-NLKKKIQKNKSLESQISELKKQNNQLKDNIEKKqqeinE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 197 LGQQLQLKVQRLHDIETENQKLRETLEEYNKEfaeVKNQEVTIKALKEKIreyeQTLKNQAETIALEKEQKLQNDFAE-- 274
Cdd:TIGR04523 244 KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE---LEQNNKKIKELEKQL----NQLKSEISDLNNQKEQDWNKELKSel 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 275 --KERKLQETQmsttSKLEEAEHKVQSLQ---TALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQraevaqrE 349
Cdd:TIGR04523 317 knQEKKLEEIQ----NQISQNNKIISQLNeqiSQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQ-------E 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 350 AETLREQLSSanhslqLASQIQKAPDVEQaievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLEQ 429
Cdd:TIGR04523 386 IKNLESQIND------LESKIQNQEKLNQ--------QKDEQIKKLQQEKELLEKEIERLKETIIKN----NSEIKDLTN 447
|
330 340 350
....*....|....*....|....*....|....*
gi 1622917398 430 QLSAKNSTLKQLEEKLKGQADY-EEVKKELNILKS 463
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQlKVLSRSINKIKQ 482
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
206-543 |
1.87e-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: 55.07 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 206 QRLHDIETENQKLRETLEEYNKEfaevKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQms 285
Cdd:TIGR02169 184 ENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLT-- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 286 ttsklEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSsanhslQ 365
Cdd:TIGR02169 258 -----EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLA------K 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 366 LASQIQKapdVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRensaSQISQLEQQLSAKNSTLKQLEEKL 445
Cdd:TIGR02169 327 LEAEIDK---LLAEIE-----ELEREIEEERKRRDKLTEEYAELKEELEDLR----AELEEVDKEFAETRDELKDYREKL 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 446 kgqadyEEVKKELNILKsmefapsegaGTQDAakplevlLMEKNRSLQSENAALRISNSDLSGRCAELQVRVTEAVATAT 525
Cdd:TIGR02169 395 ------EKLKREINELK----------RELDR-------LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451
|
330
....*....|....*...
gi 1622917398 526 EQRELIARLEQDLSIIQS 543
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQ 469
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
262-569 |
2.43e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 262 LEKEQKLQNDFAEKERKLQETQMS-TTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTakadEIEMIMTDLERAN 340
Cdd:TIGR02168 205 LERQAEKAERYKELKAELRELELAlLVLRLEELREELEELQEELKEAEEELEELTAELQELEE----KLEELRLEVSELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 341 QRAEVAQREAETLREQLSSANHSLQLASqiQKAPDVEQAIEVLTRSSLEV---------ELAAKEREIAQLVEDVQRLQA 411
Cdd:TIGR02168 281 EEIEELQKELYALANEISRLEQQKQILR--ERLANLERQLEELEAQLEELeskldelaeELAELEEKLEELKEELESLEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 412 SLTKLR---ENSASQISQLEQQLSAKNSTLKQLEEKLKG-QADYEEVKKELNILKSMEFAPSEGAGTQDaAKPLEVLLME 487
Cdd:TIGR02168 359 ELEELEaelEELESRLEELEEQLETLRSKVAQLELQIASlNNEIERLEARLERLEDRRERLQQEIEELL-KKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 488 KNRSLQSENAALrisnsdlsgrcAELQVRVTEAVATATEQRELIARLEQDL-----SIIQSIQRPDAEGAAEHRLEKIPE 562
Cdd:TIGR02168 438 LQAELEELEEEL-----------EELQEELERLEEALEELREELEEAEQALdaaerELAQLQARLDSLERLQENLEGFSE 506
|
....*..
gi 1622917398 563 PIKEATA 569
Cdd:TIGR02168 507 GVKALLK 513
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
216-442 |
3.11e-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: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 216 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALekEQKLQNDFAEKERKLQETQM-STTSKLEEAE 294
Cdd:COG4913 231 VEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYL--RAALRLWFAQRRLELLEAELeELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 295 HKVQSLQTALEKTRTELFDLKTKYDEettAKADEIEmimtDLERANQRAEVAQREAETLREQLSSANHSLQLAsqiqkAP 374
Cdd:COG4913 309 AELERLEARLDALREELDELEAQIRG---NGGDRLE----QLEREIERLERELEERERRRARLEALLAALGLP-----LP 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917398 375 DVEQaievltrsslevELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLE 442
Cdd:COG4913 377 ASAE------------EFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
199-629 |
5.08e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 5.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 199 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERK 278
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAE---LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 279 LQETQMSttskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAK----ADEIEMIMTDLERANQRAEVAQREAETLR 354
Cdd:COG4717 151 LEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 355 EQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLT------KLRENSASQISQLE 428
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLallfllLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 429 QQLSAKNSTLKQLEEK-------LKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKpLEVLLMEKNRSLQSENAAlri 501
Cdd:COG4717 307 LQALPALEELEEEELEellaalgLPPDLSPEELLELLDRIEELQELLREAEELEEELQ-LEELEQEIAALLAEAGVE--- 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 502 SNSDLSGRCAELQvrvtEAVATATEQRELIARLEQDLSIIQSIQRPDAEGAAEHRLEKIPEPIKEAtalfygpaapasga 581
Cdd:COG4717 383 DEEELRAALEQAE----EYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEEL-------------- 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1622917398 582 lpEGQVDSLLsiisSQRERFRARNQELEAENRLAQ--HTLQALQSELDSL 629
Cdd:COG4717 445 --EEELEELR----EELAELEAELEQLEEDGELAEllQELEELKAELREL 488
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
156-464 |
6.65e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 156 LLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVpdpvpalDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ 235
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELREL-------EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAE 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 236 EvtIKALKEKIREYEQTLKNQAETiaLEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQ-TALEKTRTELFDL 314
Cdd:PRK03918 526 E--YEKLKEKLIKLKGEIKSLKKE--LEKLEELKKKLAELEKKLDELE----EELAELLKELEELGfESVEELEERLKEL 597
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 315 KTKYDEETTAKADEIEmimtdLERANQRAEVAQREAETLREQLSSANHSLQlasqiqkapDVEQAIEVLTRSSLEVELAA 394
Cdd:PRK03918 598 EPFYNEYLELKDAEKE-----LEREEKELKKLEEELDKAFEELAETEKRLE---------ELRKELEELEKKYSEEEYEE 663
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 395 KEREIAQLVEDVQRLQAsltklrensasQISQLEQQLSAKNSTLKQLEEKLKgqaDYEEVKKELNILKSM 464
Cdd:PRK03918 664 LREEYLELSRELAGLRA-----------ELEELEKRREEIKKTLEKLKEELE---EREKAKKELEKLEKA 719
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
261-457 |
7.07e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 7.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 261 ALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERAN 340
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELE----KELAALKKEEKALLKQLAALERRIAALARRIRA----LEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 341 QRAEVAQREAETLREQLSSANHSLQLASQIQK------APDVEQAIEVLT--------RSSLEVELAAKEREIAQLVEDV 406
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPlalllsPEDFLDAVRRLQylkylapaRREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622917398 407 QRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKE 457
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
161-536 |
9.03e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 161 QGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYnkefaevKNQEVTIK 240
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEEL-------RELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 241 ALKEKIREYEQTLKNQAETIALEKEQKLQnDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKtkyDE 320
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQ-DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA---LE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 321 ETTAKADEIEMIMT-----------DLERANQRAEVAQ-------REAETLREQLSSANHSLQLASQIQKAPDVEQAIEV 382
Cdd:COG4717 243 ERLKEARLLLLIAAallallglggsLLSLILTIAGVLFlvlgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELE 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 383 LTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRE-NSASQISQLEQQLS-----AKNSTLKQLEEKLKGQADYEEVKK 456
Cdd:COG4717 323 ELLAALGLPPDLSPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAallaeAGVEDEEELRAALEQAEEYQELKE 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 457 ELNILKSmEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSDLSGRCAELQVRVtEAVATATEQRELIARLEQ 536
Cdd:COG4717 403 ELEELEE-QLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL-EQLEEDGELAELLQELEE 480
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
195-416 |
2.35e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.78 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 195 LDLGQQlQLKVQRLHdIETENQKLRETLEEYNKEFAEVKNQEVTIKA----LKEKIREYEQTLKNQAETIalekeQKLQN 270
Cdd:PHA02562 190 IDHIQQ-QIKTYNKN-IEEQRKKNGENIARKQNKYDELVEEAKTIKAeieeLTDELLNLVMDIEDPSAAL-----NKLNT 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 271 DFAEKERKLQ----ETQMST--------TSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakadeiemimtdlER 338
Cdd:PHA02562 263 AAAKIKSKIEqfqkVIKMYEkggvcptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELE--------------EI 328
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917398 339 ANQRAEvAQREAETLREQLSSANHSLQLAsqIQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKL 416
Cdd:PHA02562 329 MDEFNE-QSKKLLELKNKISTNKQSLITL--VDKAKKVKAAIE-----ELQAEFVDNAEELAKLQDELDKIVKTKSEL 398
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
240-444 |
5.32e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 49.63 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 240 KALKEKIREYEQTLKNQAETIALEKEQ-KLQNDFAEKERKL-----QETQMSTTSKLEEAE-HKVQ--SLQT-------- 302
Cdd:PHA02562 170 KLNKDKIRELNQQIQTLDMKIDHIQQQiKTYNKNIEEQRKKngeniARKQNKYDELVEEAKtIKAEieELTDellnlvmd 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 303 ------ALEKTRTELFDLKTKYdeETTAKadEIEMI---------MTDLERANQRaevaqreAETLREQLSSANHSL-QL 366
Cdd:PHA02562 250 iedpsaALNKLNTAAAKIKSKI--EQFQK--VIKMYekggvcptcTQQISEGPDR-------ITKIKDKLKELQHSLeKL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 367 ASQIQKAPDVEQAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKL---RENSASQISQLEQQLSAKNSTLKQL 441
Cdd:PHA02562 319 DTAIDELEEIMDEFNEQSKKLLELknKISTNKQSLITLVDKAKKVKAAIEELqaeFVDNAEELAKLQDELDKIVKTKSEL 398
|
...
gi 1622917398 442 EEK 444
Cdd:PHA02562 399 VKE 401
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
199-359 |
5.44e-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: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 199 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERK 278
Cdd:COG4913 274 LEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 279 LQETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLS 358
Cdd:COG4913 354 LEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA 429
|
.
gi 1622917398 359 S 359
Cdd:COG4913 430 S 430
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
217-463 |
5.69e-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: 50.07 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 217 KLRETLEEYNKEFAEVKNQEVTIKALKEKIRE--YEQTLKNQAETIALEKEQKLQNDFAEKERKLQEtqmsttsKLEEAE 294
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENrlDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE-------RLEELE 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 295 HKVQSLQTALEKTRTELFDLKTKYdEETTAKADEIEMIMTDLER--ANQRAEVAQREAETLREQLSSANHSLQlasqiqk 372
Cdd:TIGR02169 744 EDLSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEArlSHSRIPEIQAELSKLEEEVSRIEARLR------- 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 373 apdveqaievltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS----------QISQLEQQLSAKNSTLKQLE 442
Cdd:TIGR02169 816 --------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiekeienlngKKEELEEELEELEAALRDLE 881
|
250 260
....*....|....*....|..
gi 1622917398 443 EKLKG-QADYEEVKKELNILKS 463
Cdd:TIGR02169 882 SRLGDlKKERDELEAQLRELER 903
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
251-566 |
6.00e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.06 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 251 QTLKNQAETIALEKEQK-LQNDFAEKERKLQETQmSTTSKLEEAEHKvqsLQTALEKTRTELFDLKTKYDEEtTAKADEI 329
Cdd:TIGR02168 671 SILERRREIEELEEKIEeLEEKIAELEKALAELR-KELEELEEELEQ---LRKELEELSRQISALRKDLARL-EAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 330 EMIMTDLERANQRAEVAQREAETLREQLSSANHSL--QLASQIQKAPDVEQAIEVLTR--SSLEVELAAKEREIAQLVED 405
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAeaEIEELEAQIEQLKEELKALREalDELRAELTLLNEEAANLRER 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 406 VQRLQ---ASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQAdyEEVKKELNILKSMEFAPSEgAGTQDAAKPLE 482
Cdd:TIGR02168 826 LESLErriAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE--SELEALLNERASLEEALAL-LRSELEELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 483 VLLMEKNRS-LQSENAALRISNSDLSGRCAELQVRVTEAVATATEQreliARLEQDLSIIQSIQRPDAEGAAEHRLEKIP 561
Cdd:TIGR02168 903 LRELESKRSeLRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE----YSLTLEEAEALENKIEDDEEEARRRLKRLE 978
|
....*
gi 1622917398 562 EPIKE 566
Cdd:TIGR02168 979 NKIKE 983
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
208-462 |
8.56e-06 |
|
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: 49.44 E-value: 8.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 208 LHDIETENQKLRETLEEYNK---EFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQM 284
Cdd:pfam10174 201 LDQKEKENIHLREELHRRNQlqpDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVY 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 285 STTSKLeeAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKAD---EIEMIMTDLERANQRAEVAQREAETLREQLSSAN 361
Cdd:pfam10174 281 KSHSKF--MKNKIDQLKQELSKKESELLALQTKLETLTNQNSDckqHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 362 HSLQ---------------LASQIQKAPDV----EQAIEVLTR--SSLEVELAAKEREIAQLVEDVQRLQASLTklreNS 420
Cdd:pfam10174 359 SFLNkktkqlqdlteekstLAGEIRDLKDMldvkERKINVLQKkiENLQEQLRDKDKQLAGLKERVKSLQTDSS----NT 434
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1622917398 421 ASQISQLEQQLSAKNSTLKQLEEK--LKGQADYEEV---KKELNILK 462
Cdd:pfam10174 435 DTALTTLEEALSEKERIIERLKEQreREDRERLEELeslKKENKDLK 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-388 |
8.94e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 107 AKLKRELDATATVLANRQDESEQSRKRLIEQSREF--KKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAflnvykr 184
Cdd:TIGR02168 294 ANEISRLEQQKQILRERLANLERQLEELEAQLEELesKLDELAEELAELEEKLEELKEELESLEAELEELEAE------- 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 185 lidvpdpvpaldlgqqlqlkvqrLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAETIALEK 264
Cdd:TIGR02168 367 -----------------------LEELESRLEELEEQLETLRSKVAQLELQ---IASLNNEIERLEARLERLEDRRERLQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 265 EQKLQNDFAEKERKLQETQMSTTSK---LEEAEHKVQSLQTALEKTRTELFDLKTKYDeETTAKADEIEMIMTDLERANQ 341
Cdd:TIGR02168 421 QEIEELLKKLEEAELKELQAELEELeeeLEELQEELERLEEALEELREELEEAEQALD-AAERELAQLQARLDSLERLQE 499
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1622917398 342 RAEVAQRE-AETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSL 388
Cdd:TIGR02168 500 NLEGFSEGvKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRL 547
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
212-630 |
9.94e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 212 ETENQKLRETLEEYNKEFAEVKNQevtIKALKEKiREYEQTLKNQAETIALEKEQKLQ--NDFAEKERKLQETQMSTTSK 289
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEE---IERYEEQ-REQARETRDEADEVLEEHEERREelETLEAEIEDLRETIAETERE 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 290 LEEAEHKVQSLQTALEKTRTELFDLktkydeettakADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLAsq 369
Cdd:PRK02224 274 REELAEEVRDLRERLEELEEERDDL-----------LAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAH-- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 370 iqkapdvEQAIEVLTRSSLEVELAAKE-REIAQLVEDvqRLQASLTKLREnSASQISQLEQQLSAKNSTLKQLEEKLKGQ 448
Cdd:PRK02224 341 -------NEEAESLREDADDLEERAEElREEAAELES--ELEEAREAVED-RREEIEELEEEIEELRERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 449 ADY-EEVKKELNILKSMEfapsegagtqdaaKPLEVLLMEKNRSLQsENAALRisnsdLSGRCAELQVRVTEA--VATAT 525
Cdd:PRK02224 411 EDFlEELREERDELRERE-------------AELEATLRTARERVE-EAEALL-----EAGKCPECGQPVEGSphVETIE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 526 EQRELIARLEQDLSIIQS--------IQRPDAEGAAEHRLEKIPEPIKEATALfygpaapasgalpegqVDSLLSIISSQ 597
Cdd:PRK02224 472 EDRERVEELEAELEDLEEeveeveerLERAEDLVEAEDRIERLEERREDLEEL----------------IAERRETIEEK 535
|
410 420 430
....*....|....*....|....*....|....*.
gi 1622917398 598 RER---FRARNQELEAENRLAQHTLQALQSELDSLR 630
Cdd:PRK02224 536 RERaeeLRERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
149-464 |
1.17e-05 |
|
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: 49.20 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 149 LRKQVAPLLKSFQGEIDALSKRSK---EAEAAFLNVYKRLIDVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEY 225
Cdd:TIGR00618 554 ERKQRASLKEQMQEIQQSFSILTQcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH 633
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 226 NKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKErkLQETQMSTTSKLEEAEHKvqslQTALE 305
Cdd:TIGR00618 634 LQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQK--MQSEKEQLTYWKEMLAQC----QTLLR 707
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 306 KTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAET-LREQ-LSSANHSLQLASQIQKAPDVEQAIEVL 383
Cdd:TIGR00618 708 ELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTvLKARtEAHFNNNEEVTAALQTGAELSHLAAEI 787
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 384 T-----RSSLEVELAAKEREIAQLVED------------VQRLQASLTKLRENSASQIsQLEQQLSAKNSTLKQLEEKLK 446
Cdd:TIGR00618 788 QffnrlREEDTHLLKTLEAEIGQEIPSdedilnlqcetlVQEEEQFLSRLEEKSATLG-EITHQLLKYEECSKQLAQLTQ 866
|
330
....*....|....*...
gi 1622917398 447 GQADYEEVKKELNILKSM 464
Cdd:TIGR00618 867 EQAKIIQLSDKLNGINQI 884
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
107-461 |
1.27e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 107 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAA-FLNVYKRL 185
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEeYEKLKEKL 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 186 IDVPdpvpaldlGQQLQLK--VQRLHDIETENQKLRETLEEYNKEFAEVKNQEV-----TIKALKEKIREYEQtlknqae 258
Cdd:PRK03918 535 IKLK--------GEIKSLKkeLEKLEELKKKLAELEKKLDELEEELAELLKELEelgfeSVEELEERLKELEP------- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 259 tiALEKEQKLQNDFAEKERKLQEtQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEiemIMTDLER 338
Cdd:PRK03918 600 --FYNEYLELKDAEKELEREEKE-LKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELRE---EYLELSR 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 339 ANQRAEVAQREAETLREQLSSAnhslqlasqiqkAPDVEQAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQAsltKLR 417
Cdd:PRK03918 674 ELAGLRAELEELEKRREEIKKT------------LEKLKEELEEREKAKKELEKLEKALErVEELREKVKKYKA---LLK 738
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1622917398 418 ENSASQISQLEQQLSAK-------NSTLKQLEEKLKGQADYEEVKKELNIL 461
Cdd:PRK03918 739 ERALSKVGEIASEIFEEltegkysGVRVKAEENKVKLFVVYQGKERPLTFL 789
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
321-543 |
2.20e-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: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 321 ETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRS----SLEVELAAKE 396
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQrrleLLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 397 REIAQLVEDVQRLQASLTKLRE-----------NSASQISQLEQQLSAKNSTLKQLEEKLKGQADYeevkkelniLKSME 465
Cdd:COG4913 302 AELARLEAELERLEARLDALREeldeleaqirgNGGDRLEQLEREIERLERELEERERRRARLEAL---------LAALG 372
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917398 466 FAPSEGAgtqdaakplEVLLmeknrSLQSENAALRisnSDLSGRCAELQVRVTEAVATATEQRELIARLEQDLSIIQS 543
Cdd:COG4913 373 LPLPASA---------EEFA-----ALRAEAAALL---EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLER 433
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
208-505 |
2.31e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.12 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 208 LHDIETENQKLRETLEEYNKEFAevKNQEVTI--------KALKEKIREYEQTLKNqAETIALEKEQKLQNDFAEKERKL 279
Cdd:TIGR01612 988 LNDYEAKNNELIKYFNDLKANLG--KNKENMLyhqfdekeKATNDIEQKIEDANKN-IPNIEIAIHTSIYNIIDEIEKEI 1064
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 280 -QETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKydEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQls 358
Cdd:TIGR01612 1065 gKNIELLNKEILEEAEINITNFNEIKEKLKHYNFDDFGK--EENIKYADEINKIKDDIKNLDQKIDHHIKALEEIKKK-- 1140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 359 SANHSLQLASQIQKAPDVeqAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQASLTKLrensASQISQLEQQLSA----K 434
Cdd:TIGR01612 1141 SENYIDEIKAQINDLEDV--ADKAISNDDPE-EIEKKIENIVTKIDKKKNIYDEIKKL----LNEIAEIEKDKTSleevK 1213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622917398 435 NSTL---KQLEEKLKGQADyEEVKKELNILKSMEfAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSD 505
Cdd:TIGR01612 1214 GINLsygKNLGKLFLEKID-EEKKKSEHMIKAME-AYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDD 1285
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
107-445 |
2.49e-05 |
|
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: 47.91 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 107 AKLKRELDATATVLANRQDESEqsrkRLIEQSREFKKNTPEDlRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNV---YK 183
Cdd:pfam12128 304 DELNGELSAADAAVAKDRSELE----ALEDQHGAFLDADIET-AAADQEQLPSWQSELENLEERLKALTGKHQDVtakYN 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 184 RLIdvpdpvpaLDLGQQLQLKVQRLHDiETENQKlretlEEYNKEFAEVKNQ-EVTIKALKEKIREYEQTLKNQAETIAL 262
Cdd:pfam12128 379 RRR--------SKIKEQNNRDIAGIKD-KLAKIR-----EARDRQLAVAEDDlQALESELREQLEAGKLEFNEEEYRLKS 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 263 E-KEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAkadeiemimtdLERANQ 341
Cdd:pfam12128 445 RlGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEA-----------LRQASR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 342 RAEVAQREAETLREQLSSANHSLqLASQIQKAPDVEQAI------EVLTRSSLEVEL----AAKEREIAQLVEDVQRLQA 411
Cdd:pfam12128 514 RLEERQSALDELELQLFPQAGTL-LHFLRKEAPDWEQSIgkvispELLHRTDLDPEVwdgsVGGELNLYGVKLDLKRIDV 592
|
330 340 350
....*....|....*....|....*....|....*
gi 1622917398 412 -SLTKLRENSASQISQLEQQLSAKNSTLKQLEEKL 445
Cdd:pfam12128 593 pEWAASEEELRERLDKAEEALQSAREKQAAAEEQL 627
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
107-457 |
2.88e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 107 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDlRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLI 186
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED-KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA 1440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 187 DVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLE--EYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEK 264
Cdd:PTZ00121 1441 EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 265 EQKLQN-DFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMImtDLERANQRA 343
Cdd:PTZ00121 1521 AKKADEaKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKA--EEARIEEVM 1598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 344 EVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSslEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQ 423
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK--EAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK 1676
|
330 340 350
....*....|....*....|....*....|....
gi 1622917398 424 ISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKE 457
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKK 1710
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
108-462 |
3.28e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 108 KLKRELDATATVLANRQDESEQSRKRLIEQsREFKKNTPEDLRKQVApllkSFQGEIDALsKRSKEAEAAFLNVYKRLID 187
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKET-IIKNNSEIKDLTNQDS----VKELIIKNL-DNTRESLETQLKVLSRSIN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 188 VPDPvPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNqevTIKALKEKIREYEQTLKNQAETIaLEKEQK 267
Cdd:TIGR04523 479 KIKQ-NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE---KIEKLESEKKEKESKISDLEDEL-NKDDFE 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 268 LQNDFAEKErkLQETQmsttSKLEEAEHKvqslQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQ 347
Cdd:TIGR04523 554 LKKENLEKE--IDEKN----KEIEELKQT----QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 348 REAETLREQ----LSSANHSLQLASQIQ--------KAPDVEQAIEvltrsslevELAAKEREIAQLVEDvqRLQASLTK 415
Cdd:TIGR04523 624 KENEKLSSIikniKSKKNKLKQEVKQIKetikeirnKWPEIIKKIK---------ESKTKIDDIIELMKD--WLKELSLH 692
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1622917398 416 LRENSASQIsqleqqlsaKNSTLKQLEEKlkgqadYEEVKKELNILK 462
Cdd:TIGR04523 693 YKKYITRMI---------RIKDLPKLEEK------YKEIEKELKKLD 724
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
103-447 |
3.32e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 47.77 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 103 CVAGAKLKRELDATATVLANRQDESEQSRKRlieQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaAFLNVY 182
Cdd:COG5022 830 KKLRETEEVEFSLKAEVLIQKFGRSLKAKKR---FSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKL-VNLELE 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 183 KRLIDV-----PDPVPALDLGQQLQLKVQRLHD-IETENQKLRetleEYNKEFAEVKNQEVtIKALKEKIREYEQTLKNQ 256
Cdd:COG5022 906 SEIIELkkslsSDLIENLEFKTELIARLKKLLNnIDLEEGPSI----EYVKLPELNKLHEV-ESKLKETSEEYEDLLKKS 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 257 AETI-----ALEKEQKLQNDFAEKeRKLQETQMSTTSKLEEAEHKVQSLQTALEktrtelfdlktKYDEETTAKAdeIEM 331
Cdd:COG5022 981 TILVregnkANSELKNFKKELAEL-SKQYGALQESTKQLKELPVEVAELQSASK-----------IISSESTELS--ILK 1046
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 332 IMTDLERAN-QRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEReiaqlVEDVQRLQ 410
Cdd:COG5022 1047 PLQKLKGLLlLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPAN-----VLQFIVAQ 1121
|
330 340 350
....*....|....*....|....*....|....*..
gi 1622917398 411 ASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKG 447
Cdd:COG5022 1122 MIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDG 1158
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
276-464 |
4.13e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 276 ERKLQETQMSTT---SKLEEAEHKVQSLQTALE--KTRTELFDLktkyDEETTAKADEIEMIMTDLERANQRAEVAQREA 350
Cdd:COG3206 167 ELRREEARKALEfleEQLPELRKELEEAEAALEefRQKNGLVDL----SEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 351 ETLREQLSSANHSL-------QLASQIQKAPDVEQAIEVLTRSSLE-----VELAAKEREI-AQLVEDVQRLQASLTKLR 417
Cdd:COG3206 243 AALRAQLGSGPDALpellqspVIQQLRAQLAELEAELAELSARYTPnhpdvIALRAQIAALrAQLQQEAQRILASLEAEL 322
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622917398 418 ENSASQISQLEQQLSAKNSTLKQLEEKlkgQADYEEVKKELNILKSM 464
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPEL---EAELRRLEREVEVAREL 366
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
145-447 |
4.68e-05 |
|
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: 47.14 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 145 TPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDpvpaldlgQQLQLKVQRLHDIETENQKLRETLEE 224
Cdd:pfam12128 615 SAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFD--------EKQSEKDKKNKALAERKDSANERLNS 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 225 YNKEfaevknqevtIKALKEKIREYEQTLKNQAETIALEKEQKLQNdfAEKERKLQETQMSTTSKLEEAEHKVQslQTAL 304
Cdd:pfam12128 687 LEAQ----------LKQLDKKHQAWLEEQKEQKREARTEKQAYWQV--VEGALDAQLALLKAAIAARRSGAKAE--LKAL 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 305 EKTRTElfDLKTK-YDEETTAK-ADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQlasqIQKApDVEQAIEv 382
Cdd:pfam12128 753 ETWYKR--DLASLgVDPDVIAKlKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLA----TQLS-NIERAIS- 824
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622917398 383 ltrsslevelaakereiaqlvedvqRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKG 447
Cdd:pfam12128 825 -------------------------ELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRG 864
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
147-339 |
5.52e-05 |
|
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: 45.82 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 147 EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAfLNVYKRLIDvpdpvpalDLGQQLQLKVQRLHDI-ETENQKL-RETLEE 224
Cdd:cd22656 113 EEAKKTIKALLDDLLKEAKKYQDKAAKVVDK-LTDFENQTE--------KDQTALETLEKALKDLlTDEGGAIaRKEIKD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 225 YNKEFAevKNQEVTIKALKEKIREYEQTLKNQAETIAleKEQKLQNDFaekerKLQETQM-STTSKLEEAEHKVQSLQTA 303
Cdd:cd22656 184 LQKELE--KLNEEYAAKLKAKIDELKALIADDEAKLA--AALRLIADL-----TAADTDLdNLLALIGPAIPALEKLQGA 254
|
170 180 190
....*....|....*....|....*....|....*.
gi 1622917398 304 LEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERA 339
Cdd:cd22656 255 WQAIATDLDSLKDLLEDDIS-KIPAAILAKLELEKA 289
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
263-645 |
6.59e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.27 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 263 EKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRtELFDLKTKYDEETTAKADEIEMIMTDLERANQR 342
Cdd:pfam05557 48 DRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLN-EKESQLADAREVISCLKNELSELRRQIQRAELE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 343 AEVAQREAETLREQL----------SSANHSLQ-----LASQIQKAPDVEQAIEVLTRSSLEVELAAKERE-IAQLVEDV 406
Cdd:pfam05557 127 LQSTNSELEELQERLdllkakaseaEQLRQNLEkqqssLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELArIPELEKEL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 407 QRLQASLTKLRENSASqISQLEQQLSAKNSTLKQLE----EKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPL- 481
Cdd:pfam05557 207 ERLREHNKHLNENIEN-KLLLKEEVEDLKRKLEREEkyreEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRi 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 482 ------EVLLMEKNRSLQSENAALRISNSDLSGRCAELQVRVTEAVATATEQRELIARLEQDLSII--------QSIQRP 547
Cdd:pfam05557 286 eqlqqrEIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLtkerdgyrAILESY 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 548 DAEGAAEHRLEKIPEPIKEATALFYGPAAPASGAlpEGQVDSLLSIISSQRERFRA--------RNQELEAENRLAQHTL 619
Cdd:pfam05557 366 DKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEM--EAQLSVAEEELGGYKQQAQTlerelqalRQQESLADPSYSKEEV 443
|
410 420
....*....|....*....|....*.
gi 1622917398 620 QALQSELDSLRADNIKLFEKIKFLQS 645
Cdd:pfam05557 444 DSLRRKLETLELERQRLREQKNELEM 469
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
215-530 |
9.18e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.90 E-value: 9.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 215 NQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQA-ETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEA 293
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 294 EHK-VQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLE--RANQRAE--VAQREAETLREQLSSANHSLQ--- 365
Cdd:pfam07111 138 SQReLEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLEtkRAGEAKQlaEAQKEAELLRKQLSKTQEELEaqv 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 366 -LASQIQKAPDvEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQAS--LTKLRENSASQISQL-EQQLSAKNSTLKQL 441
Cdd:pfam07111 218 tLVESLRKYVG-EQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATveLLQVRVQSLTHMLALqEEELTRKIQPSDSL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 442 EEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSDLSGRCAELQVrvtEAV 521
Cdd:pfam07111 297 EPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEV---ERM 373
|
....*....
gi 1622917398 522 ATATEQREL 530
Cdd:pfam07111 374 SAKGLQMEL 382
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
285-480 |
9.19e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 9.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 285 STTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEettaKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL 364
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 365 Q-------------LASQIQKAPDVEQAIEVLTRSSLEV--ELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQ 429
Cdd:COG3883 96 YrsggsvsyldvllGSESFSDFLDRLSALSKIADADADLleELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622917398 430 QLSAKNSTLKQLEEKlkgQADYEEVKKELNILKSMEFAPSEGAGTQDAAKP 480
Cdd:COG3883 176 QQAEQEALLAQLSAE---EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
240-507 |
1.03e-04 |
|
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: 46.12 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 240 KALKEKIREYEQTLKNQAETIALEK-EQKLQNDFAEKERKLQETQmsttsKLEEAEhkvqsLQTALEKTRTELFDLKTKY 318
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLEELKLqELKLKEQAKKALEYYQLKE-----KLELEE-----EYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 319 DEETTAKADEIEMImtdleraNQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKERE 398
Cdd:pfam02463 243 QELLRDEQEEIESS-------KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 399 IAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILKSmefapSEGAGTQDAA 478
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK-----LESERLSSAA 390
|
250 260
....*....|....*....|....*....
gi 1622917398 479 KPLEVLLMEKNRSLQSENAALRISNSDLS 507
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLED 419
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
107-335 |
1.21e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.90 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 107 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEaaflnvykrli 186
Cdd:PTZ00121 1589 AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE----------- 1657
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 187 dvPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKnqAETIALEKEQ 266
Cdd:PTZ00121 1658 --ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK--AEEENKIKAE 1733
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917398 267 KLQNDFAEKERKLQETQmsttsKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD 335
Cdd:PTZ00121 1734 EAKKEAEEDKKKAEEAK-----KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
206-536 |
1.25e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 206 QRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKEQKLQNDFAEKERKLQETQMS 285
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNLV--QTALRQQEKIERYQADLEELEERLEEQNEV 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 286 T---TSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTaKADEIEMIMTDLERANQ--------------RAEVAQR 348
Cdd:PRK04863 371 VeeaDEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQT-RAIQYQQAVQALERAKQlcglpdltadnaedWLEEFQA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 349 EAETLREQLSSANHSLQLASQIQKApdVEQAIEVLTRSSLEVelaakEREIAQlvedvQRLQASLTKLRE--NSASQISQ 426
Cdd:PRK04863 450 KEQEATEELLSLEQKLSVAQAAHSQ--FEQAYQLVRKIAGEV-----SRSEAW-----DVARELLRRLREqrHLAEQLQQ 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 427 LEQQLSAknstlkqLEEKLKGQADYEEVKKELNilKSMEFAPSEGAGTQDAAKPLEVLLmeknRSLQSENAALRISNSDL 506
Cdd:PRK04863 518 LRMRLSE-------LEQRLRQQQRAERLLAEFC--KRLGKNLDDEDELEQLQEELEARL----ESLSESVSEARERRMAL 584
|
330 340 350
....*....|....*....|....*....|
gi 1622917398 507 SGRCAELQVRVTEAVATATEQRELIARLEQ 536
Cdd:PRK04863 585 RQQLEQLQARIQRLAARAPAWLAAQDALAR 614
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
155-460 |
2.41e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 155 PLLKSFQGEIDALSKRsKEAEAAFLNVYKRLIDvpdpvpALDLGQQLQlkvqrlhDIETENQKLRETLEEYNKEFAEVKN 234
Cdd:PRK11281 36 PTEADVQAQLDALNKQ-KLLEAEDKLVQQDLEQ------TLALLDKID-------RQKEETEQLKQQLAQAPAKLRQAQA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 235 QevtIKALKEKIreyEQTLKNQAETIALEKeqkLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKTRTELFdl 314
Cdd:PRK11281 102 E---LEALKDDN---DEETRETLSTLSLRQ---LESRLAQTLDQLQNAQ----NDLAEYNSQLVSLQTQPERAQAALY-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 315 ktkydeettakadeiemimtdlerANQraevaQREAEtLREQLSSANHSlqlasqiQKAPDVEQaievltRSSLEVELAA 394
Cdd:PRK11281 167 ------------------------ANS-----QRLQQ-IRNLLKGGKVG-------GKALRPSQ------RVLLQAEQAL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 395 KEREIA---QLVEDVQRLQASLTKLRENSASQISQLEQQL-------SAKNstLKQLEEKLKGQADYEE---------VK 455
Cdd:PRK11281 204 LNAQNDlqrKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLqllqeaiNSKR--LTLSEKTVQEAQSQDEaariqanplVA 281
|
....*
gi 1622917398 456 KELNI 460
Cdd:PRK11281 282 QELEI 286
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
206-348 |
2.60e-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: 43.37 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 206 QRLHDIETENQKLRETLEEYNKEF----AEVKNQEVTIKALKEKIREYEQTL---KNQAETIALEKEQklqnDFAEKERK 278
Cdd:COG1579 31 AELAELEDELAALEARLEAAKTELedleKEIKRLELEIEEVEARIKKYEEQLgnvRNNKEYEALQKEI----ESLKRRIS 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622917398 279 LQETQMS-TTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTdlERANQRAEVAQR 348
Cdd:COG1579 107 DLEDEILeLMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA--EREELAAKIPPE 175
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
199-644 |
2.74e-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: 44.72 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 199 QQLQLKVQRLHDIETENQKLRETLEeynKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQN------DF 272
Cdd:pfam15921 120 QEMQMERDAMADIRRRESQSQEDLR---NQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEirsilvDF 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 273 AEKERK--LQETQMSTT--SKLEEAEHKV-QSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTD-LERANQRAEVA 346
Cdd:pfam15921 197 EEASGKkiYEHDSMSTMhfRSLGSAISKIlRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQhQDRIEQLISEH 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 347 QREAETLREQLSSANhslqlasqiQKAPDVEQAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQ 426
Cdd:pfam15921 277 EVEITGLTEKASSAR---------SQANSIQSQLEIIQEQARN-QNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEE 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 427 LEQQLSAKNSTLKQ--------------LEEKL-KGQADYEEVKKELNILKSM-EFAPSEGAGTQDAAKPLEVLLMEKNR 490
Cdd:pfam15921 347 LEKQLVLANSELTEarterdqfsqesgnLDDQLqKLLADLHKREKELSLEKEQnKRLWDRDTGNSITIDHLRRELDDRNM 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 491 SLQSENAALRISNSDLSGRCAelqvRVTEAVATATEQRELIARLEQDLSIIQSIQRPDAE--GAAEHRLEKIPEPIKEAT 568
Cdd:pfam15921 427 EVQRLEALLKAMKSECQGQME----RQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEelTAKKMTLESSERTVSDLT 502
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622917398 569 alfygpaapASGALPEGQVDSLLSIISSQRERFRARNQELEAENRLAQHtLQALQSELDSLRadnIKLFEKIKFLQ 644
Cdd:pfam15921 503 ---------ASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDH-LRNVQTECEALK---LQMAEKDKVIE 565
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
204-544 |
2.90e-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: 44.34 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 204 KVQRLHDIETENQKLRETLEEYNKEFaevKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQ 283
Cdd:pfam17380 235 KMERRKESFNLAEDVTTMTPEYTVRY---NGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKARE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 284 MSTTSKLEEAEHKVQSL------------QTALEKTRT-ELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA 350
Cdd:pfam17380 312 VERRRKLEEAEKARQAEmdrqaaiyaeqeRMAMERERElERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 351 ETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEvelAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQ 430
Cdd:pfam17380 392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQE---EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 431 LSAKNSTLKQLEEKLKGQADYEEVKKELnILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSDLSGRC 510
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKI-LEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQE 547
|
330 340 350
....*....|....*....|....*....|....
gi 1622917398 511 AELQVRVTEAVATATEQRELIARLEQDLSIIQSI 544
Cdd:pfam17380 548 MEERRRIQEQMRKATEERSRLEAMEREREMMRQI 581
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
114-449 |
3.14e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 114 DATATVLANRQDE----SEQSRKRLIEQ--SREFKKNTPEDLRKQVAPLlksfQGEIDALSKRSKEAEAAFLNVYKRLID 187
Cdd:PRK02224 306 DADAEAVEARREEledrDEELRDRLEECrvAAQAHNEEAESLREDADDL----EERAEELREEAAELESELEEAREAVED 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 188 VPDPVPALDlgQQLQLKVQRLHDIETEnqklRETLEEYNKEFAEVKNqevtikALKEKIREYEQTLKNQAETIALEKEQK 267
Cdd:PRK02224 382 RREEIEELE--EEIEELRERFGDAPVD----LGNAEDFLEELREERD------ELREREAELEATLRTARERVEEAEALL 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 268 LQNDFAEKERKLQETQMSTTskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAK--ADEIEMIMTDLERANQRAEV 345
Cdd:PRK02224 450 EAGKCPECGQPVEGSPHVET--IEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVeaEDRIERLEERREDLEELIAE 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 346 AQREAETLREQLSSANHSLQ-LASQIQKAPDVEQAIEVLTRSSLEvELAAKEREIAQLVEDVQRLQ--ASLTKLRENSAS 422
Cdd:PRK02224 528 RRETIEEKRERAEELRERAAeLEAEAEEKREAAAEAEEEAEEARE-EVAELNSKLAELKERIESLEriRTLLAAIADAED 606
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1622917398 423 QISQLEQQ--------------LSAKNSTLKQLEEKLKGQA 449
Cdd:PRK02224 607 EIERLREKrealaelnderrerLAEKRERKRELEAEFDEAR 647
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
206-408 |
3.15e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 206 QRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQklqndfAEKERKLQETQmS 285
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREI------AELEAELERLD-A 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 286 TTSKLEEAEHKVQSLQTALEKTRTELFDLKTKY---DEETTAKADEIEMIMTDLERANQRAEVAQRE-AETLREQLSSAN 361
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIgrlEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALGDA 762
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622917398 362 HSLQLASQIQKApdveqaievltRSSLEVELAAKEREIAQLVEDVQR 408
Cdd:COG4913 763 VERELRENLEER-----------IDALRARLNRAEEELERAMRAFNR 798
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
207-630 |
3.85e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 207 RLHDIETENQKLRETLEEYNKEFAE--VKNQEVTIKALKEKI---REYEQTLKNQAETIalEKEQKLQND-FAEKERKLQ 280
Cdd:pfam15921 246 QLEALKSESQNKIELLLQQHQDRIEqlISEHEVEITGLTEKAssaRSQANSIQSQLEII--QEQARNQNSmYMRQLSDLE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 281 ETQMSTTSKLEEA----EHKVQSLQTALEKTRTELFDLKTKYDE---ETTAKADEIEMIMTDLERANQRAEVAQREAETL 353
Cdd:pfam15921 324 STVSQLRSELREAkrmyEDKIEELEKQLVLANSELTEARTERDQfsqESGNLDDQLQKLLADLHKREKELSLEKEQNKRL 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 354 REQLSSANHSL-QLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQ--ASLTKLRENSASQISQLEQQ 430
Cdd:pfam15921 404 WDRDTGNSITIdHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEkvSSLTAQLESTKEMLRKVVEE 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 431 LSAKNSTLKQ-----------LEEKLKG----QADYEEVKKELNI-LKSMEFAPSEGAGTQDAAKPLEVL---LMEKNRS 491
Cdd:pfam15921 484 LTAKKMTLESsertvsdltasLQEKERAieatNAEITKLRSRVDLkLQELQHLKNEGDHLRNVQTECEALklqMAEKDKV 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 492 L-----QSEN------------AALRISNSDLSGRCAELQVRVTEAVATATEQRELIARLEQDLSIIQsIQRPDAEGAAE 554
Cdd:pfam15921 564 IeilrqQIENmtqlvgqhgrtaGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE-LEKVKLVNAGS 642
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622917398 555 HRLEKIPEPIKEATALFYGPAAPASgalpegQVDSLLSIISSQRERFRARNQELEAENRLAQHTLQALQSELDSLR 630
Cdd:pfam15921 643 ERLRAVKDIKQERDQLLNEVKTSRN------ELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTR 712
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
339-586 |
4.31e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 4.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 339 ANQRAEVAQREAETLREQLSSANHslQLASQIQKAPDVEQAIEvltrsSLEVELAAKEREIAQLVEDVQRLQASLTKLRE 418
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEK--ELAALKKEEKALLKQLA-----ALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 419 nsasQISQLEQQLSAKNSTLKQLEEKL--KGQADYEEVkkelnILKSMEFAPSEGAGT-----QDAAKPLEVLLMEKNRS 491
Cdd:COG4942 91 ----EIAELRAELEAQKEELAELLRALyrLGRQPPLAL-----LLSPEDFLDAVRRLQylkylAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 492 LQSENAALRISNSDLSGRCAELQVRVTEAVATATEQRELIARLEQDLSIIQsiQRPDAEGAAEHRLEKIPEPIKEATALF 571
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA--AELAELQQEAEELEALIARLEAEAAAA 239
|
250
....*....|....*
gi 1622917398 572 YGPAAPASGALPEGQ 586
Cdd:COG4942 240 AERTPAAGFAALKGK 254
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
207-316 |
4.39e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.08 E-value: 4.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 207 RLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAET---IALEKEQKLQNDFA---EKERKLQ 280
Cdd:smart00787 138 RMKLLEGLKEGLDENLEGLKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQlkqLEDELEDCDPTELDrakEKLKKLL 217
|
90 100 110
....*....|....*....|....*....|....*.
gi 1622917398 281 ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKT 316
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELNT 253
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
214-459 |
5.92e-04 |
|
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: 43.42 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 214 ENQKLRETLE---EYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKL 290
Cdd:pfam02463 174 ALKKLIEETEnlaELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEI 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 291 EEAEhKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA--ETLREQLSSANHSLQLAS 368
Cdd:pfam02463 254 ESSK-QEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDeeKLKESEKEKKKAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 369 QIQKAPDVEQAIEVLTRSSLEVELA--AKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLK 446
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEeeELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLE 412
|
250
....*....|...
gi 1622917398 447 GQADYEEVKKELN 459
Cdd:pfam02463 413 LARQLEDLLKEEK 425
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
107-357 |
6.55e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 107 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTP-----EDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNV 181
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaeaEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 182 YKRlidvpdpvpALDLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETI- 260
Cdd:TIGR02168 816 NEE---------AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLe 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 261 -ALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDLERA 339
Cdd:TIGR02168 887 eALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY---SLTLEEAEALENKI 963
|
250
....*....|....*...
gi 1622917398 340 NQRAEVAQREAETLREQL 357
Cdd:TIGR02168 964 EDDEEEARRRLKRLENKI 981
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
161-457 |
6.73e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 161 QGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPAL-----DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQ 235
Cdd:pfam10174 344 QTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLageirDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKER 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 236 evtIKALKEKIREYEQTLKNQAETIAlEKE---QKLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELF 312
Cdd:pfam10174 424 ---VKSLQTDSSNTDTALTTLEEALS-EKEriiERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLI 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 313 DLKtkydEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANhslQLASQIQKAPDVEQAIevltrSSLEVEL 392
Cdd:pfam10174 500 DLK----EHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH---NAEEAVRTNPEINDRI-----RLLEQEV 567
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917398 393 AAKEREIAQLVEDVQRLQASLtKLRENSAS----QISQLE---------QQLSAKNSTLKQLEEKLKGQADYEEVKKE 457
Cdd:pfam10174 568 ARYKEESGKAQAEVERLLGIL-REVENEKNdkdkKIAELEsltlrqmkeQNKKVANIKHGQQEMKKKGAQLLEEARRR 644
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
208-467 |
8.62e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.89 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 208 LHDIETENQKLRETL----EEYNKEFAEVKNQEVTIKALKEKIREYEQTL-KNQAETIALE-KEQKLQNDFAEKERKLQE 281
Cdd:pfam10174 249 IRDLEDEVQMLKTNGllhtEDREEEIKQMEVYKSHSKFMKNKIDQLKQELsKKESELLALQtKLETLTNQNSDCKQHIEV 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 282 TQMSTTSKLEEA---EHKVQSLQTALEKTRTeLFDLKTKY----DEETTAKADEIEMIMTDLERANQRAEVAQREAETLR 354
Cdd:pfam10174 329 LKESLTAKEQRAailQTEVDALRLRLEEKES-FLNKKTKQlqdlTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQ 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 355 EQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQ-------ASLTKLRENSASQISQL 427
Cdd:pfam10174 408 EQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDrerleelESLKKENKDLKEKVSAL 487
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1622917398 428 EQQLSAKNSTLKQLEEKLKGQAdyEEVKKELNILKSMEFA 467
Cdd:pfam10174 488 QPELTEKESSLIDLKEHASSLA--SSGLKKDSKLKSLEIA 525
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
202-357 |
8.76e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 202 QLKVQRLhDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLknQAETIALEKEQKLQNDFAEKERKLQE 281
Cdd:COG1340 75 ELKEERD-ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ--QTEVLSPEEEKELVEKIKELEKELEK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 282 TQMS--TTSKLEEAEHKVQSLQTALEKTR---TELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQ 356
Cdd:COG1340 152 AKKAleKNEKLKELRAELKELRKEAEEIHkkiKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEE 231
|
.
gi 1622917398 357 L 357
Cdd:COG1340 232 I 232
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
196-537 |
9.08e-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: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 196 DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEvtikalkekireyEQTLKNQAETIALEKEQKLQNDFAEK 275
Cdd:pfam15921 500 DLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEG-------------DHLRNVQTECEALKLQMAEKDKVIEI 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 276 ERKLQETQMSTTSKLEEAEHKVQSLQTALEKT----RTELFDLKTKYDEEtTAKADEIEMIMTDLERanQRAEVAQREAE 351
Cdd:pfam15921 567 LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEindrRLELQEFKILKDKK-DAKIRELEARVSDLEL--EKVKLVNAGSE 643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 352 TLREQLSSANHSLQLASQIQKAPD----VEQAIEVLTR-------------SSLEVELAAKEREIAQLVEDVQRLQAS-- 412
Cdd:pfam15921 644 RLRAVKDIKQERDQLLNEVKTSRNelnsLSEDYEVLKRnfrnkseemetttNKLKMQLKSAQSELEQTRNTLKSMEGSdg 723
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 413 -LTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKgqadyeEVKKELNILKSMEfapsegagtQDAAKPLEVLLMEKNRs 491
Cdd:pfam15921 724 hAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMT------NANKEKHFLKEEK---------NKLSQELSTVATEKNK- 787
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1622917398 492 LQSENAALRISNSDLSGRCAELQVRVTEAVATATEQRELIARLEQD 537
Cdd:pfam15921 788 MAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQE 833
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
120-305 |
1.03e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 120 LANRQDESEQSRKRLieqsREFKKNT----PEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPAL 195
Cdd:COG3206 184 LPELRKELEEAEAAL----EEFRQKNglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 196 DLGQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYEQTLKNQAET---IALEKEQKLQNDF 272
Cdd:COG3206 260 LQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQ---IAALRAQLQQEAQRILASLEAeleALQAREASLQAQL 336
|
170 180 190
....*....|....*....|....*....|...
gi 1622917398 273 AEKERKLQETQmSTTSKLEEAEHKVQSLQTALE 305
Cdd:COG3206 337 AQLEARLAELP-ELEAELRRLEREVEVARELYE 368
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
220-441 |
1.11e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 41.05 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 220 ETLEEYNKEFAEVKN--QEVT------IKALKEKIREyeqtLKNQAEtialEKEQKLQNDFAEKERkLQEtqmsttsKLE 291
Cdd:pfam13851 1 ELMKNHEKAFNEIKNyyNDITrnnlelIKSLKEEIAE----LKKKEE----RNEKLMSEIQQENKR-LTE-------PLQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 292 EAEHKVQSLQTAL---EKTRTELfdlktkydEETTAKADEIEMIMTDLERAN----QRAEVAQREAETLREQLSSANHSL 364
Cdd:pfam13851 65 KAQEEVEELRKQLenyEKDKQSL--------KNLKARLKVLEKELKDLKWEHevleQRFEKVERERDELYDKFEAAIQDV 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622917398 365 QLASQiQKAPDVEQAIEVLTRsslevELAAKEREIAQLvedvqrLQASltKLRENSASQISQ-LEQQLSAKNSTLKQL 441
Cdd:pfam13851 137 QQKTG-LKNLLLEKKLQALGE-----TLEKKEAQLNEV------LAAA--NLDPDALQAVTEkLEDVLESKNQLIKDL 200
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
219-446 |
1.22e-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: 42.34 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 219 RETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKnqaetiALEK-EQKLQNDFAEKERKLQETQMSTTSKLEEAEHKV 297
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIK------ALKSrKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNH 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 298 QSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQ---------REAETLREQLSSANHSLQLAS 368
Cdd:TIGR00606 311 QRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQehirardslIQSLATRLELDGFERGPFSER 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 369 QIQKAPDVE---QAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKL 445
Cdd:TIGR00606 391 QIKNFHTLVierQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSS 470
|
.
gi 1622917398 446 K 446
Cdd:TIGR00606 471 D 471
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
198-443 |
1.26e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 198 GQQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIalekeQKLQNDFAEKER 277
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI-----RELEERIEELKK 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 278 KLQ--ETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKtKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLRE 355
Cdd:PRK03918 274 EIEelEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE-KRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 356 QLSSANHSLQLasqiqkapdVEQAIEVLTR-SSLEVELAAKERE-IAQLVEDVQRLQASLTKLRENSASQISQLEQQLSA 433
Cdd:PRK03918 353 RLEELEERHEL---------YEEAKAKKEElERLKKRLTGLTPEkLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250
....*....|
gi 1622917398 434 KNSTLKQLEE 443
Cdd:PRK03918 424 LKKAIEELKK 433
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
197-465 |
1.68e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 41.73 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 197 LGQQLQLKVQRLHDIETENQKLRETLEEynKEfaevknqevtikALKEKIREYEQTLKNQAETIALEKEQkLQNDFAEKE 276
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEVDALRLRLEE--KE------------SFLNKKTKQLQDLTEEKSTLAGEIRD-LKDMLDVKE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 277 RK----------LQETQMSTTSKLEEAEHKVQSLQTALEKTRTELfdlkTKYDEETTAKADEIEMIMTDLERANQ--RAE 344
Cdd:pfam10174 394 RKinvlqkkienLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTAL----TTLEEALSEKERIIERLKEQREREDRerLEE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 345 VAQ--REAETLREQLSSANHslQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIA--QLVEDVQRLQASLTKLRENS 420
Cdd:pfam10174 470 LESlkKENKDLKEKVSALQP--ELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAveQKKEECSKLENQLKKAHNAE 547
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1622917398 421 ---------ASQISQLEQQLSAKNstlkqlEEKLKGQAdyeEVKKELNILKSME 465
Cdd:pfam10174 548 eavrtnpeiNDRIRLLEQEVARYK------EESGKAQA---EVERLLGILREVE 592
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
208-645 |
1.74e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 208 LHDIETENQKLRETLEEYNKEFAEVKNQ----EVTIKALKEKIREYEQTLKNqaetiaLEKEQKLQNDFAEKERKLQETQ 283
Cdd:TIGR04523 154 LEKLNNKYNDLKKQKEELENELNLLEKEklniQKNIDKIKNKLLKLELLLSN------LKKKIQKNKSLESQISELKKQN 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 284 MSTTSKLEEAEHKVQSLQTALEKTRTELFDLKtkydeettakaDEIEMIMTDLERANQRAEVAQREAETLREQLSsanhs 363
Cdd:TIGR04523 228 NQLKDNIEKKQQEINEKTTEISNTQTQLNQLK-----------DEQNKIKKQLSEKQKELEQNNKKIKELEKQLN----- 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 364 lQLASQIQkapDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLSAKNSTLKQLEE 443
Cdd:TIGR04523 292 -QLKSEIS---DLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNE----QISQLKKELTNSESENSEKQR 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 444 KLkgqadyEEVKKELNILKsmefapsegagtqdaakplevllmEKNRSLQSENAALRISNSDLsgrcaELQVRVTEAVAT 523
Cdd:TIGR04523 364 EL------EEKQNEIEKLK------------------------KENQSYKQEIKNLESQINDL-----ESKIQNQEKLNQ 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 524 ATEQRelIARLEQDLSII-QSIQRPDAEGAAEHrlEKIPEPIKEATALfygpaapasgalpEGQVDSLLSIISSQRERFr 602
Cdd:TIGR04523 409 QKDEQ--IKKLQQEKELLeKEIERLKETIIKNN--SEIKDLTNQDSVK-------------ELIIKNLDNTRESLETQL- 470
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1622917398 603 arnQELEAENRLAQHTLQALQ-------SELDSLRADNIKLFEKIKFLQS 645
Cdd:TIGR04523 471 ---KVLSRSINKIKQNLEQKQkelkskeKELKKLNEEKKELEEKVKDLTK 517
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
211-443 |
1.99e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 211 IETENQKLRETLEEYNKEFAEVKNQevtIKALKEKIREYeqtlKNQAETIALEKEQKLqndFAEKERKLQETQMSTTSKL 290
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKE---LEEAEAALEEF----RQKNGLVDLSEEAKL---LLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 291 EEAEHKVQSLQTALEKT----------------RTELFDLKTKYDEE-TTAKADEIEMIMTDLERANQRAEVAQREAETL 353
Cdd:COG3206 236 AEAEARLAALRAQLGSGpdalpellqspviqqlRAQLAELEAELAELsARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 354 REQLSsanhslQLASQIQKAPDVEQAIEVLTRSSLEveLAAKEREIAQLVEDVQRLQASLTKLREnsasQISQLEQQLSA 433
Cdd:COG3206 316 ASLEA------ELEALQAREASLQAQLAQLEARLAE--LPELEAELRRLEREVEVARELYESLLQ----RLEEARLAEAL 383
|
250
....*....|
gi 1622917398 434 KNSTLKQLEE 443
Cdd:COG3206 384 TVGNVRVIDP 393
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
107-462 |
2.03e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 107 AKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLI 186
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 187 DVPDPVPALDLGQQLQLKVQRLHDIETENQKLRETLEEYnKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQ 266
Cdd:COG1196 505 GFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA-LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIR 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 267 KLQNDFAEKERKLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVA 346
Cdd:COG1196 584 ARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 347 QREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENsasqisQ 426
Cdd:COG1196 664 GGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE------L 737
|
330 340 350
....*....|....*....|....*....|....*.
gi 1622917398 427 LEQQLSAKNSTLKQLEEKLKGQADYEEVKKELNILK 462
Cdd:COG1196 738 LEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
216-570 |
2.15e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 216 QKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDfAEKERKLQETQMSTTSKlEEAEH 295
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE-EERDDLLAEAGLDDADA-EAVEA 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 296 KVQSLQTALEKTRTELFDLKTkydeETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHslQLASQIQKAPD 375
Cdd:PRK02224 315 RREELEDRDEELRDRLEECRV----AAQAHNEEAESLREDADDLEERAEELREEAAELESELEEARE--AVEDRREEIEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 376 VEQAIEVL---------TRSSLEVELAAKEREIAQLVEDVQRLQASLTKLREN------------------------SAS 422
Cdd:PRK02224 389 LEEEIEELrerfgdapvDLGNAEDFLEELREERDELREREAELEATLRTARERveeaealleagkcpecgqpvegspHVE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 423 QISQLEQQLSAKNSTLKQLEEKLkgqadyEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSEN---AAL 499
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEV------EEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKReraEEL 542
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622917398 500 RISNSDLSGRCAELQVRVTEAVATATEQRELIARLEQDLSIIQSiqRPDAEGAAEHRLEKIPEPIKEATAL 570
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKE--RIESLERIRTLLAAIADAEDEIERL 611
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
142-449 |
2.84e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 142 KKNTPEDLRKQVAPLLkSFQGEIDALSKRSKEAEAAFLNVYKRLIDVPDPVPALDLGQQ-------LQLKVQRLH----- 209
Cdd:pfam12128 191 KEGKFRDVKSMIVAIL-EDDGVVPPKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQefntlesAELRLSHLHfgyks 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 210 ---DIETENQKLRETLEEYNKEFAEVKNQevtikaLKEKIREYEQTLKNQAETIALEKEQ---------KLQNDFAEKER 277
Cdd:pfam12128 270 detLIASRQEERQETSAELNQLLRTLDDQ------WKEKRDELNGELSAADAAVAKDRSElealedqhgAFLDADIETAA 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 278 KLQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETtakADEIEMIMTDLE-----RANQRAE---VAQRE 349
Cdd:pfam12128 344 ADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQN---NRDIAGIKDKLAkireaRDRQLAVaedDLQAL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 350 AETLREQLSSANHSL------------QLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQL-VEDVQRLQASLTKL 416
Cdd:pfam12128 421 ESELREQLEAGKLEFneeeyrlksrlgELKLRLNQATATPELLLQLENFDERIERAREEQEAANAeVERLQSELRQARKR 500
|
330 340 350
....*....|....*....|....*....|...
gi 1622917398 417 RENSASQISQLEQQLSAKNSTLKQLEEKLKGQA 449
Cdd:pfam12128 501 RDQASEALRQASRRLEERQSALDELELQLFPQA 533
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
339-635 |
3.07e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 339 ANQRAEVAQREAETLREQLSSANhSLQLASQIQKA--PDVEQAIEVLTR--------SSLEVELAAKEREIAQLVEDVQR 408
Cdd:PRK11281 27 ARAASNGDLPTEADVQAQLDALN-KQKLLEAEDKLvqQDLEQTLALLDKidrqkeetEQLKQQLAQAPAKLRQAQAELEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 409 LQASLTK-LRENSASQ-ISQLEQQLSAKNSTLKQLEEKLkgqADY-----------EEVKKEL--NILKSMEFApSEGAG 473
Cdd:PRK11281 106 LKDDNDEeTRETLSTLsLRQLESRLAQTLDQLQNAQNDL---AEYnsqlvslqtqpERAQAALyaNSQRLQQIR-NLLKG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 474 TQDAAKPLEVLLMEKnrsLQSENAALRISNSDlsgRCAELQVRvTEAVATATEQREL----IARLEQDLSIIQSIqrpda 549
Cdd:PRK11281 182 GKVGGKALRPSQRVL---LQAEQALLNAQNDL---QRKSLEGN-TQLQDLLQKQRDYltarIQRLEHQLQLLQEA----- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 550 egAAEHRLEKIPEPIKEATalfygpaapASGALPEGQVDSLLSiissqrerfrarnQELEAENRLAQHTLQALQsELDSL 629
Cdd:PRK11281 250 --INSKRLTLSEKTVQEAQ---------SQDEAARIQANPLVA-------------QELEINLQLSQRLLKATE-KLNTL 304
|
....*.
gi 1622917398 630 RADNIK 635
Cdd:PRK11281 305 TQQNLR 310
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
239-449 |
3.09e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 239 IKALKEKIREYEQTLKNqaetiALEKEQKLQNDFAEKERKLQETQmsttSKLEEAEHKVQSLQTALEKTRTELFDLKTKY 318
Cdd:COG3883 18 IQAKQKELSELQAELEA-----AQAELDALQAELEELNEEYNELQ----AELEALQAEIDKLQAEIAEAEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 319 DE------ETTAKADEIEMIM--TDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEV 390
Cdd:COG3883 89 GEraralyRSGGSVSYLDVLLgsESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917398 391 ELAAKEREIAQLvedvQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEKLKGQA 449
Cdd:COG3883 169 AKAELEAQQAEQ----EALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
201-465 |
3.09e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 201 LQLKVQRLHDIETENQKLRETLEEYNKEFAE---------VKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQK-LQN 270
Cdd:pfam05483 445 LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDlktelekekLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEdIIN 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 271 DFAEKERKLQEtqmsttskLEEAEHKVQSLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREA 350
Cdd:pfam05483 525 CKKQEERMLKQ--------IENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 351 ETLREQLSSANHSLQLASQIQKAPDVEQAIEV-------LTRSSLEVELAAKEREIAQLVEDVQRlQASLTKLRENS--- 420
Cdd:pfam05483 597 NNLKKQIENKNKNIEELHQENKALKKKGSAENkqlnayeIKVNKLELELASAKQKFEEIIDNYQK-EIEDKKISEEKlle 675
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917398 421 --------ASQISQLEQQLSA----KNSTLKQLEEKLKGQAD--YEEVKKELNILKSME 465
Cdd:pfam05483 676 evekakaiADEAVKLQKEIDKrcqhKIAEMVALMEKHKHQYDkiIEERDSELGLYKNKE 734
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
212-510 |
3.16e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.11 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 212 ETENQKLRETLEEYNKEFAEVKNQEVTIKALK-EKIREYEQTLKNQAETIALEKEQklqNDFAEKERKLQETQMSTTSKL 290
Cdd:pfam02463 218 KLELEEEYLLYLDYLKLNEERIDLLQELLRDEqEEIESSKQEIEKEEEKLAQVLKE---NKEEEKEKKLQEEELKLLAKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 291 EEaehkVQSLQTALEKTRTELFDLKTKYDEETTAKAD-EIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQ 369
Cdd:pfam02463 295 EE----ELKSELLKLERRKVDDEEKLKESEKEKKKAEkELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQ 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 370 IQKAPDV------EQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSAS------QISQLEQQLSAKNST 437
Cdd:pfam02463 371 LEEELLAkkklesERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELeileeeEESIELKQGKLTEEK 450
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622917398 438 LKQLEEKLKGQADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSDLSGRC 510
Cdd:pfam02463 451 EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGR 523
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
161-447 |
3.31e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 161 QGEIDALSKRSKEAEAAFLNVYKRLIDVpdpVPALDLGQ----QLQLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQE 236
Cdd:PRK04863 375 DEQQEENEARAEAAEEEVDELKSQLADY---QQALDVQQtraiQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 237 vtiKALKEKIREYEQTLkNQAETIALEKEQKLQ---------------NDFAEKERKLQETQMSTTSkLEEAEHKVQSLQ 301
Cdd:PRK04863 452 ---QEATEELLSLEQKL-SVAQAAHSQFEQAYQlvrkiagevsrseawDVARELLRRLREQRHLAEQ-LQQLRMRLSELE 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 302 TALEKTRTeLFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSL-QLASQIQK----APDV 376
Cdd:PRK04863 527 QRLRQQQR-AERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLeQLQARIQRlaarAPAW 605
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622917398 377 EQAIEVLTRSSLEVELAAKERE-IAQLVEDVQRLQASLTKLRENSASQISQLEQQLS-------AKNSTLKQLEEKLKG 447
Cdd:PRK04863 606 LAAQDALARLREQSGEEFEDSQdVTEYMQQLLERERELTVERDELAARKQALDEEIErlsqpggSEDPRLNALAERFGG 684
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
199-542 |
4.69e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.54 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 199 QQLQLKVQRLHDIETENQKLRETLEEYNKEFAEVknqevtikaLKEKIREYEQTlknQAETIALEKEQKLQNDFAEKERK 278
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQL---------CEEKNALQEQL---QAETELCAEAEEMRARLAARKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 279 LQETQMSTTSKLEEAEHKVQSLQTALEKTRTELFDLKTKYDEE-------------TTAKADEIEMIMTDLERANQRaev 345
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEeaarqklqlekvtTEAKIKKLEEDILLLEDQNSK--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 346 AQREAETLREQLSSANHSLQLASQIQKAPDVEQAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSA---S 422
Cdd:pfam01576 150 LSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAelqA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 423 QISQLEQQLSAKNSTLKQLEEKLKgqadyEEVKKELNILKSMefapsegagtqdaaKPLEVLLMEKNRSLQSENAALRIS 502
Cdd:pfam01576 230 QIAELRAQLAKKEEELQAALARLE-----EETAQKNNALKKI--------------RELEAQISELQEDLESERAARNKA 290
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1622917398 503 NS---DLSGRCAELQVRVTEAVATATEQRELIARLEQDLSIIQ 542
Cdd:pfam01576 291 EKqrrDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELK 333
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
214-311 |
4.70e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 214 ENQKLRETLEEynkefaEVKNQEVTIKALKEKIREYEQTLKNQAEtiALEKeqklqndfaeKERKLQETQMSTTSKLEEA 293
Cdd:PRK12704 65 EIHKLRNEFEK------ELRERRNELQKLEKRLLQKEENLDRKLE--LLEK----------REEELEKKEKELEQKQQEL 126
|
90
....*....|....*...
gi 1622917398 294 EHKVQSLQTALEKTRTEL 311
Cdd:PRK12704 127 EKKEEELEELIEEQLQEL 144
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
122-570 |
5.46e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 122 NRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAflNVYKRLIDvpdpvpalDLGQQL 201
Cdd:PTZ00121 1087 NRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKA--EEARKAED--------AKRVEI 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 202 QLKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKAlkEKIREYEQTLKNQAETIALEKEQklqndfAEKERKLQE 281
Cdd:PTZ00121 1157 ARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKA--EDARKAEAARKAEEERKAEEARK------AEDAKKAEA 1228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 282 TQmsttsKLEEAEHKVQSLQTAlEKTRtelfdlktkyDEETTAKADEIEMIMTDLERANQRAEVAqREAETLREQlssan 361
Cdd:PTZ00121 1229 VK-----KAEEAKKDAEEAKKA-EEER----------NNEEIRKFEEARMAHFARRQAAIKAEEA-RKADELKKA----- 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 362 HSLQLASQIQKAPDVEQAIEVLTRSslevELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQL 441
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKA----EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 442 EEKLKG--------QADYEEVKKELNILKSMEFAPSEGAGTQDAAKPLEVLLMEKNRSLQSENAALRISNSDLSGRCAEL 513
Cdd:PTZ00121 1363 EEKAEAaekkkeeaKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEE 1442
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 514 QVRVTEAVATATEQR---ELIARLEQDLSIIQSIQRPDAEGAAEHRLEKIPEPIKEATAL 570
Cdd:PTZ00121 1443 AKKADEAKKKAEEAKkaeEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA 1502
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
121-366 |
5.61e-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: 40.13 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 121 ANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLNVYKRLIDVpdpvpaldLGQQ 200
Cdd:pfam09731 231 VEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVLKEDNLLSNDDLNSLIAHAHREIDQ--------LSKK 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 201 LQ-LKVQRLHDIETENQKLRETLE----------EYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQ 269
Cdd:pfam09731 303 LAeLKKREEKHIERALEKQKEELDklaeelsarlEEVRAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLK 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 270 NDFAEKERKLQETQMsttskleeaehkvQSLQTALEKTRtelfDLKTKYDEETTAKADEIEMIMT---DLERANQRAEVA 346
Cdd:pfam09731 383 DVLVEQEIELQREFL-------------QDIKEKVEEER----AGRLLKLNELLANLKGLEKATSshsEVEDENRKAQQL 445
|
250 260
....*....|....*....|
gi 1622917398 347 QREAETLREQLSSANHSLQL 366
Cdd:pfam09731 446 WLAVEALRSTLEDGSADSRP 465
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
132-356 |
5.85e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 132 KRLIEQSREFKKNTPEDLRKqvapllksfqgeidalSKRSKEAEAAFLNVYKRLIDVPDPVPALDL--GQQLQLKVQRLH 209
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRK----------------AEEAKKAEEARIEEVMKLYEEEKKMKAEEAkkAEEAKIKAEELK 1626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 210 DIETENQK---LRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKNQAETIALEKEQKLQNDFAEKERKLQETQMST 286
Cdd:PTZ00121 1627 KAEEEKKKveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE 1706
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622917398 287 TSKLEEAE-HKVQSLQTALEKTRTELFDLKTKyDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQ 356
Cdd:PTZ00121 1707 LKKKEAEEkKKAEELKKAEEENKIKAEEAKKE-AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKE 1776
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
388-669 |
6.67e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 388 LEVELAAKEREIAQLVEDVQRLQAsltklrensasQISQLEQQLSAknstLKQLEEKLKGQADYEEVKKELnilksmefa 467
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEA-----------ELDALQERREA----LQRLAEYSWDEIDVASAEREI--------- 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 468 psegagtqdaakplevllmeknRSLQSENAALRISNSDLsgrcAELQVRVTEAVATATEQRELIARLEQDlsiiqsiqrp 547
Cdd:COG4913 671 ----------------------AELEAELERLDASSDDL----AALEEQLEELEAELEELEEELDELKGE---------- 714
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 548 daEGAAEHRLEKIPEPIKEATALFYGPAAPASGALpegqvdsllsiissqRERFRARNQELEAENRLAQHtLQALQSELD 627
Cdd:COG4913 715 --IGRLEKELEQAEEELDELQDRLEAAEDLARLEL---------------RALLEERFAAALGDAVEREL-RENLEERID 776
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1622917398 628 SLRADNIKLFEKI-----KFLQSYPGRgSSSDDTELRYSSQYEERLD 669
Cdd:COG4913 777 ALRARLNRAEEELeramrAFNREWPAE-TADLDADLESLPEYLALLD 822
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
216-433 |
7.97e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 39.65 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 216 QKLRETLEEYNKEFAEVkNQEVTIKALKEKIREYEQTLKNQAETiaLEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEH 295
Cdd:PRK10929 82 AELRQQLNNERDEPRSV-PPNMSTDALEQEILQVSSQLLEKSRQ--AQQEQDRAREISDSLSQLPQQQTEARRQLNEIER 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 296 KVQSL--------QTALEKTRTELFDLKtkydeettAKADEIEMIMTDL----ERANQRAEVAQREAETLREQLSSANHs 363
Cdd:PRK10929 159 RLQTLgtpntplaQAQLTALQAESAALK--------ALVDELELAQLSAnnrqELARLRSELAKKRSQQLDAYLQALRN- 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 364 lQLASQIQKapDVEQAIEvltrsslEVELAAKE---------------REIAQ-LVEDVQRLQASLTKLREnSASQISQL 427
Cdd:PRK10929 230 -QLNSQRQR--EAERALE-------STELLAEQsgdlpksivaqfkinRELSQaLNQQAQRMDLIASQQRQ-AASQTLQV 298
|
....*.
gi 1622917398 428 EQQLSA 433
Cdd:PRK10929 299 RQALNT 304
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
210-463 |
8.89e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 39.62 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 210 DIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIReyeqTLKNQaETIALEKEQKLQND--FAEKERKLQETQMSTT 287
Cdd:TIGR04523 48 ELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIK----DLNDK-LKKNKDKINKLNSDlsKINSEIKNDKEQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 288 ----SKLEEAEHKVQSLQ----TALEKTRTELFDLKTKYDEETTakadEIEMIMTDLERANQRAEVAQREAETLREQLSS 359
Cdd:TIGR04523 123 evelNKLEKQKKENKKNIdkflTEIKKKEKELEKLNNKYNDLKK----QKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 360 ANHSL-QLASQIQKAPDVEQAIEVL--TRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLE---QQLSA 433
Cdd:TIGR04523 199 LELLLsNLKKKIQKNKSLESQISELkkQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSekqKELEQ 278
|
250 260 270
....*....|....*....|....*....|
gi 1622917398 434 KNSTLKQLEEKLKgqadyeEVKKELNILKS 463
Cdd:TIGR04523 279 NNKKIKELEKQLN------QLKSEISDLNN 302
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
310-462 |
9.80e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 39.07 E-value: 9.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622917398 310 ELFD-LKTKYDEETTAKADEIEMIMTDLERANQRAEV--AQREAETLREQLSSANHSLQlasQIQKapDVEQAIEVLTRS 386
Cdd:pfam06160 45 EKFEeWRKKWDDIVTKSLPDIEELLFEAEELNDKYRFkkAKKALDEIEELLDDIEEDIK---QILE--ELDELLESEEKN 119
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622917398 387 SLEVElaakereiaQLVEDVQRLQASLTKLRENSASQISQLEQQLSAKNSTLKQLEEkLKGQADYEEVKKELNILK 462
Cdd:pfam06160 120 REEVE---------ELKDKYRELRKTLLANRFSYGPAIDELEKQLAEIEEEFSQFEE-LTESGDYLEAREVLEKLE 185
|
|
| |
