|
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 ... |
409-638 |
6.06e-84 |
|
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: 264.53 E-value: 6.06e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 409 ELKKSVDQLKQQIATLKEANEKLETDLEKVENVS---PHFNETASMMSGVTRQMnnRTSHKMSPTSSIIGIPEDGELSG- 484
Cdd:pfam08172 1 TLQEELSSLNAELEEQQELNAKLENDLLKVQDEAsnaFSFNDASSAGSGVSRYP--PSGGRRSPTSSIISGFEPSESSSs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 485 NQSTILPIVTKQRDRFRSRNMDLEKQLRQGNSEKGKLKLEISKLKGDNTKLYERIRYLQSYNNNNAPVNQS--------- 555
Cdd:pfam08172 79 SDSSILPIVTSQRDRFRQRNAELEEELRKQFETISSLRQEIASLQKDNLKLYEKTRYLQSYNRGGGGGTKSssstsssas 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 556 -------TERIDVESQYSRVYDESLHPMANFRQNELNhYKNKKLSALEKLFSSFAKVILQNKMTRMVFLFYCIGLHGLVF 628
Cdd:pfam08172 159 aygnnpnPSDVEALDKYRKAYEESLNPFAAFRGRESE-RAYKRLSPLERLVLSLTRLVLANRTSRNLFFFYCLALHLLVF 237
|
250
....*....|
gi 549740 629 MMSMYVINIS 638
Cdd:pfam08172 238 FTLYYVSNSS 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-436 |
1.22e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 225 QKEVSTRIAEYNlvtQELETTQARIY-----QLEKRNEELSGALAKATSE-AEKETELHAKELKLNQLESENALLSASYE 298
Cdd:TIGR02168 208 QAEKAERYKELK---AELRELELALLvlrleELREELEELQEELKEAEEElEELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 299 QERK---STSHAINEL-------KEQLNSVVAESESYKSELETVRRKLNNYsdynkiKEELSALKKIEFGVNEDdsdndi 368
Cdd:TIGR02168 285 ELQKelyALANEISRLeqqkqilRERLANLERQLEELEAQLEELESKLDEL------AEELAELEEKLEELKEE------ 352
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549740 369 rsedkndntfESSLLSANKKLQATLAEYRSKSTAQEEERNELKKSVDQLKQQIATLKEANEKLETDLE 436
Cdd:TIGR02168 353 ----------LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
122-437 |
2.12e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 122 ELKEKISYLEDKLAKYADYETLKSRLLDLEQSSAKTLAKRLTAKTQEINSTWEEKgrnwKEREADLLKQLTNVQEQNKAL 201
Cdd:COG1196 197 ELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL----EAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 202 EAKIsknidiegngnedgdQENNQKEVSTRIAEYNLVTQELETTQARIYQLEKRNEELSGALAKATSEAEKETELHAKEL 281
Cdd:COG1196 273 RLEL---------------EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 282 KLNQLESENALLSASYEQERKSTSHAINELKEQLNSVVAESESYKSELETVRRKLNNysDYNKIKEELSALKKIEfgvNE 361
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA--AAELAAQLEELEEAEE---AL 412
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549740 362 DDSDNDIRSEDKNDNTFESSLLSANKKLQATLAEYRSKSTAQEEERNELKKSVDQLKQQIATLKEANEKLETDLEK 437
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
18-441 |
1.20e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 18 LTNLQRELDADVIEIKDketlsLNSRKSLATETKKFKKLEPEEKLNNVNKI---IKQYQREIDNLTQRSKFSEKVLFDVY 94
Cdd:PRK03918 167 LGEVIKEIKRRIERLEK-----FIKRTENIEELIKEKEKELEEVLREINEIsseLPELREELEKLEKEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 95 EKLSEAPDPQPLLQSSLEKLGKIDDS-KELKEKISYLEDK------LAKYAD-YETLKSRLLDLEQSSAKtLAKRLTAKT 166
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERiEELKKEIEELEEKvkelkeLKEKAEeYIKLSEFYEEYLDELRE-IEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 167 QEIN---------STWEEKGRNWKEREADLLKQLTNVQEQNKALEAKISKNIDIEG-----NGNEDGDQENNQKEVSTRI 232
Cdd:PRK03918 321 EEINgieerikelEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkrlTGLTPEKLEKELEELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 233 AEynlVTQELETTQARIYQLEKRNEELSGALAKATSeAEKETELHAKELKlnqlESENALLSASYEQERKSTSHAINELK 312
Cdd:PRK03918 401 EE---IEEEISKITARIGELKKEIKELKKAIEELKK-AKGKCPVCGRELT----EEHRKELLEEYTAELKRIEKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 313 EQLNSVVAESESYKSELETVRRKLNNYSDYNKIKEELSALKKIEFgvneddsdndirsedkndntfessllsanKKLQAT 392
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNL-----------------------------EELEKK 523
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 549740 393 LAEYRSkstaQEEERNELKKSVDQLKQQIATLKEANEKLETDLEKVENV 441
Cdd:PRK03918 524 AEEYEK----LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDEL 568
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
233-430 |
1.75e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 233 AEYNLVTQELETTQ---ARIYQLEKRNEELSGALAKATSE-AEKETELHA-KELKLNQLESENALLS-ASYEQERKSTSH 306
Cdd:PRK11281 56 AEDKLVQQDLEQTLallDKIDRQKEETEQLKQQLAQAPAKlRQAQAELEAlKDDNDEETRETLSTLSlRQLESRLAQTLD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 307 AINELKEQLNSVVAESESYKSELETVRRKLNNYSdynKIKEELSALKKiefgvNEDDSDNDIRSEDKNDNTFESSLLSAN 386
Cdd:PRK11281 136 QLQNAQNDLAEYNSQLVSLQTQPERAQAALYANS---QRLQQIRNLLK-----GGKVGGKALRPSQRVLLQAEQALLNAQ 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 549740 387 KKLQATLAEYRSKSTA-QEEERNELKKSVDQLKQQIATLKEA-NEK 430
Cdd:PRK11281 208 NDLQRKSLEGNTQLQDlLQKQRDYLTARIQRLEHQLQLLQEAiNSK 253
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
24-548 |
5.72e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 24 ELDADVIEIKDKETLSLNSRKSLATETKKFKKlepeeKLNNVNKIIKQYQREIDNLTQRSKFSEKVLFDVYEKLSEAPDP 103
Cdd:TIGR04523 100 KLNSDLSKINSEIKNDKEQKNKLEVELNKLEK-----QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 104 QPLLQSSLEKLGK-IDDSKELKEKISYLEDKLAKY-ADYETLKSRLLDLEQSSaKTLAKRLTAKTQEINSTWEEKGRNWK 181
Cdd:TIGR04523 175 LNLLEKEKLNIQKnIDKIKNKLLKLELLLSNLKKKiQKNKSLESQISELKKQN-NQLKDNIEKKQQEINEKTTEISNTQT 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 182 EreadlLKQLTNvqEQNKALEAKISKNIDIEGNGNEDGDQENNQKEVSTRIAEYNLVTQElETTQARIYQLEKRNEELSG 261
Cdd:TIGR04523 254 Q-----LNQLKD--EQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ-DWNKELKSELKNQEKKLEE 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 262 ALAKATSEAEKETELhakELKLNQLESEnallSASYEQERKSTSHAINELKEQLNSVVAESESYKSELETVRRKLNNYSD 341
Cdd:TIGR04523 326 IQNQISQNNKIISQL---NEQISQLKKE----LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLES 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 342 YNKIKEELSALKkiefgvneddsDNDIRSEDKNDNTFE---SSLLSANKKLQATLAEYRSKSTAQEEERNELKKSVDQLK 418
Cdd:TIGR04523 399 KIQNQEKLNQQK-----------DEQIKKLQQEKELLEkeiERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 419 QQIATLKEANEKLETDLEKVENVSPHFNETASMMSGVTRQMNNRTSHKMSPTSSIIGIPEDGELSGNQ--STILPIVTK- 495
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEkeSKISDLEDEl 547
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 549740 496 QRDRFRSRNMDLEKQLRQGNSEKGKLKLEISKLKGDNTKLYERIRYLQSYNNN 548
Cdd:TIGR04523 548 NKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
16-335 |
1.03e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 16 ADLTNLQRELDADVIEIKDKETLSLNSRKSLATETKKFKKLEPE-----EKLNNVNKIIKQYQREIDNLTQRSKFSEKVL 90
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEieqleQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 91 FDVYEKLSEAPDPQPLLQSSLEKL-GKIDDS--KELKEKISYLEDKLAKyadyetLKSRLLDLEQ-----SSAKTLAKRL 162
Cdd:TIGR02169 761 KELEARIEELEEDLHKLEEALNDLeARLSHSriPEIQAELSKLEEEVSR------IEARLREIEQklnrlTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 163 TAKTQEINSTWEEKGRNWKEREADLLKQLTNVQEQNKALEAKI----SKNIDIEGNGNE-DGDQENNQKEVSTRIAEYNL 237
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALrdleSRLGDLKKERDElEAQLRELERKIEELEAQIEK 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 238 VTQELETTQARIYQLEKRNEELSGALAKATSEAEKET-------ELHAKELKLNQLESENALLsasyEQERKSTSHAINE 310
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsledvqaELQRVEEEIRALEPVNMLA----IQEYEEVLKRLDE 990
|
330 340
....*....|....*....|....*...
gi 549740 311 LKEQLNSVVAESESYK---SELETVRRK 335
Cdd:TIGR02169 991 LKEKRAKLEEERKAILeriEEYEKKKRE 1018
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
95-437 |
1.55e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 95 EKLSEAPDPQPLLQSSLEKLGKIddSKELKEKISYLEDKLAKYADYETL---KSRLLDLEQSSAKTLAKRLTAKTQEIN- 170
Cdd:pfam15921 458 ESLEKVSSLTAQLESTKEMLRKV--VEELTAKKMTLESSERTVSDLTASlqeKERAIEATNAEITKLRSRVDLKLQELQh 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 171 -STWEEKGRNwKEREADLLK-QLTNVQEQNKALEAKISKNIDIEG-NGNEDGDQENNQKEVSTRIAEYNLVTQELETTQ- 246
Cdd:pfam15921 536 lKNEGDHLRN-VQTECEALKlQMAEKDKVIEILRQQIENMTQLVGqHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKd 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 247 ---ARIYQLEKRNEELSGALAK----------ATSEAEKETELHAKELK-----LNQLESENALLSASYEQERKSTSHAI 308
Cdd:pfam15921 615 kkdAKIRELEARVSDLELEKVKlvnagserlrAVKDIKQERDQLLNEVKtsrneLNSLSEDYEVLKRNFRNKSEEMETTT 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 309 NELKEQLNSVvaesesyKSELETVRRKLNNY--SDYNKIKEELSALKKIEFGVNEDDSdndIRSEDKndnTFESSLLSAN 386
Cdd:pfam15921 695 NKLKMQLKSA-------QSELEQTRNTLKSMegSDGHAMKVAMGMQKQITAKRGQIDA---LQSKIQ---FLEEAMTNAN 761
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 549740 387 KKlQATLAEYRSKSTAQ----EEERNELKKSVDQLKQQIATLKEANEKLETDLEK 437
Cdd:pfam15921 762 KE-KHFLKEEKNKLSQElstvATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
107-289 |
1.56e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 107 LQSSLEKLGK------IDDSKELKEKISYLEDKLAKYADYETLKSRLLDLEQsSAKTLAKRLTAKTQEIN--STWEEKGR 178
Cdd:COG4717 51 LEKEADELFKpqgrkpELNLKELKELEEELKEAEEKEEEYAELQEELEELEE-ELEELEAELEELREELEklEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 179 NWKEREAdLLKQLTNVQEQNKALEAKISkniDIEGNGNEDGDQENNQKEVSTRIAEynLVTQELETTQARIYQLEKRNEE 258
Cdd:COG4717 130 LYQELEA-LEAELAELPERLEELEERLE---ELRELEEELEELEAELAELQEELEE--LLEQLSLATEEELQDLAEELEE 203
|
170 180 190
....*....|....*....|....*....|..
gi 549740 259 LSGALAKATSEAEK-ETELHAKELKLNQLESE 289
Cdd:COG4717 204 LQQRLAELEEELEEaQEELEELEEELEQLENE 235
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
62-539 |
2.47e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 62 LNNVNKIIKQYQREIDNLTQRSKFSEKVLFDVYEKLSEAP-------DPQPLLQSSLEKLGKIDDSK-----ELKEKISY 129
Cdd:PRK01156 185 IDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSieynnamDDYNNLKSALNELSSLEDMKnryesEIKTAESD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 130 LEDKLAKYADYETLKSRLLDLEQSSAktlakrlTAKTQEINSTWEEKGR--NWKEREADLLKQLTNVQEQNKALEAKISK 207
Cdd:PRK01156 265 LSMELEKNNYYKELEERHMKIINDPV-------YKNRNYINDYFKYKNDieNKKQILSNIDAEINKYHAIIKKLSVLQKD 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 208 NIDIEGNGNEDGDQENNQKEVSTRIAEYNLVTQELETTQARIYQLEKRNEELSGALAKATSEAEKETELHAKEL-----K 282
Cdd:PRK01156 338 YNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELneinvK 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 283 LNQLESENALLSASYEQERKST------------------------SHAINELKEQLNSVVAESESYKSELETVRRKLNN 338
Cdd:PRK01156 418 LQDISSKVSSLNQRIRALRENLdelsrnmemlngqsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 339 YSDYNKIKEELSALKKIEFGVNEDDSDNDIRSEDKNDNTFESSLLSANKKLQATLAEYRSKSTAQEEERNE--------- 409
Cdd:PRK01156 498 KIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTswlnalavi 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 410 -------LKKSVDQLKQQIATLKEANEKLETDLEKVENVSPHFNETASMMSGVTRQMNNRTSHKMSPTSSIIGIPED--G 480
Cdd:PRK01156 578 slidietNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNykK 657
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549740 481 ELSGNQSTI--LPIVTKQRDRFRSRNMDLEKQLRQGNSEKGKLKLEISKLKGDNTKLYERI 539
Cdd:PRK01156 658 QIAEIDSIIpdLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI 718
|
|
| |
|
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 ... |
409-638 |
6.06e-84 |
|
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: 264.53 E-value: 6.06e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 409 ELKKSVDQLKQQIATLKEANEKLETDLEKVENVS---PHFNETASMMSGVTRQMnnRTSHKMSPTSSIIGIPEDGELSG- 484
Cdd:pfam08172 1 TLQEELSSLNAELEEQQELNAKLENDLLKVQDEAsnaFSFNDASSAGSGVSRYP--PSGGRRSPTSSIISGFEPSESSSs 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 485 NQSTILPIVTKQRDRFRSRNMDLEKQLRQGNSEKGKLKLEISKLKGDNTKLYERIRYLQSYNNNNAPVNQS--------- 555
Cdd:pfam08172 79 SDSSILPIVTSQRDRFRQRNAELEEELRKQFETISSLRQEIASLQKDNLKLYEKTRYLQSYNRGGGGGTKSssstsssas 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 556 -------TERIDVESQYSRVYDESLHPMANFRQNELNhYKNKKLSALEKLFSSFAKVILQNKMTRMVFLFYCIGLHGLVF 628
Cdd:pfam08172 159 aygnnpnPSDVEALDKYRKAYEESLNPFAAFRGRESE-RAYKRLSPLERLVLSLTRLVLANRTSRNLFFFYCLALHLLVF 237
|
250
....*....|
gi 549740 629 MMSMYVINIS 638
Cdd:pfam08172 238 FTLYYVSNSS 247
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-436 |
1.22e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 225 QKEVSTRIAEYNlvtQELETTQARIY-----QLEKRNEELSGALAKATSE-AEKETELHAKELKLNQLESENALLSASYE 298
Cdd:TIGR02168 208 QAEKAERYKELK---AELRELELALLvlrleELREELEELQEELKEAEEElEELTAELQELEEKLEELRLEVSELEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 299 QERK---STSHAINEL-------KEQLNSVVAESESYKSELETVRRKLNNYsdynkiKEELSALKKIEFGVNEDdsdndi 368
Cdd:TIGR02168 285 ELQKelyALANEISRLeqqkqilRERLANLERQLEELEAQLEELESKLDEL------AEELAELEEKLEELKEE------ 352
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549740 369 rsedkndntfESSLLSANKKLQATLAEYRSKSTAQEEERNELKKSVDQLKQQIATLKEANEKLETDLE 436
Cdd:TIGR02168 353 ----------LESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
122-437 |
2.12e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 122 ELKEKISYLEDKLAKYADYETLKSRLLDLEQSSAKTLAKRLTAKTQEINSTWEEKgrnwKEREADLLKQLTNVQEQNKAL 201
Cdd:COG1196 197 ELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL----EAELEELEAELAELEAELEEL 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 202 EAKIsknidiegngnedgdQENNQKEVSTRIAEYNLVTQELETTQARIYQLEKRNEELSGALAKATSEAEKETELHAKEL 281
Cdd:COG1196 273 RLEL---------------EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 282 KLNQLESENALLSASYEQERKSTSHAINELKEQLNSVVAESESYKSELETVRRKLNNysDYNKIKEELSALKKIEfgvNE 361
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA--AAELAAQLEELEEAEE---AL 412
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549740 362 DDSDNDIRSEDKNDNTFESSLLSANKKLQATLAEYRSKSTAQEEERNELKKSVDQLKQQIATLKEANEKLETDLEK 437
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
59-358 |
2.16e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 59 EEKLNNVNKIIKQYQREIDNLTQR-----SKFSEKVLFdVYEKLSEAPDPQPLLQSSLEKLGKIDDSKE-LKEKISYLED 132
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAElqeleEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKQiLRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 133 KLAKYADY-ETLKSRLLDLEQS----------------SAKTLAKRLTAKTQEINSTWEEKGRNW---KEREADLLKQLT 192
Cdd:TIGR02168 317 QLEELEAQlEELESKLDELAEElaeleekleelkeeleSLEAELEELEAELEELESRLEELEEQLetlRSKVAQLELQIA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 193 NVQEQNKALEAKISkniDIEGNgNEDGDQENNQKEVSTRIAEYNLVTQELETTQARIYQLEKRNEELSGALAKATSE-AE 271
Cdd:TIGR02168 397 SLNNEIERLEARLE---RLEDR-RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREElEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 272 KETELHAKELKLNQLESENALLSASYEQERKSTSHAINELKEQ-----LNSVVAES----ESYKSELETVRRKLNNY--- 339
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQsglsgILGVLSELisvdEGYEAAIEAALGGRLQAvvv 552
|
330
....*....|....*....
gi 549740 340 SDYNKIKEELSALKKIEFG 358
Cdd:TIGR02168 553 ENLNAAKKAIAFLKQNELG 571
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
184-439 |
6.11e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.15 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 184 EADLLKQLTNVQ-EQNKALEAKISKNIDIEGNGNED-GDQENNQKEVSTRIAEYNLVTQELETTQARIYQLEKRNEELSG 261
Cdd:TIGR02169 193 IDEKRQQLERLRrEREKAERYQALLKEKREYEGYELlKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 262 ALAKATSEAEKETELHAKELK--LNQLESENALLSAS---YEQERKSTSHAINELKEQLNSVVAESESYKSELETVRRKL 336
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQLRVKekIGELEAEIASLERSiaeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 337 NnysdynKIKEELSALKKIEfgvneDDSDNDIRSEDKndntfessllsANKKLQATLAEYRSKSTAQEEERNELKKSVDQ 416
Cdd:TIGR02169 353 D------KLTEEYAELKEEL-----EDLRAELEEVDK-----------EFAETRDELKDYREKLEKLKREINELKRELDR 410
|
250 260
....*....|....*....|...
gi 549740 417 LKQQIATLKEANEKLETDLEKVE 439
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIE 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
65-439 |
6.27e-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: 52.76 E-value: 6.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 65 VNKIIKQYQRE----IDNLTQRSKFSEKV------LFDVYEKLSEApdpQPLLQSSLEKLGKIDDSKELKEKISYLEDKL 134
Cdd:TIGR02169 144 VTDFISMSPVErrkiIDEIAGVAEFDRKKekaleeLEEVEENIERL---DLIIDEKRQQLERLRREREKAERYQALLKEK 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 135 AKYADYETLKsRLLDLEQSSAKTLAK--RLTAKTQEINSTWEEKGRNWKEREADLlkqltnvqeqnKALEAKISKnidie 212
Cdd:TIGR02169 221 REYEGYELLK-EKEALERQKEAIERQlaSLEEELEKLTEEISELEKRLEEIEQLL-----------EELNKKIKD----- 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 213 gngnedgDQENNQKEVSTRIAEynlVTQELETTQARIYQLEKRNEELSGALAKAtseaekETELHAKELKLNQLESEnal 292
Cdd:TIGR02169 284 -------LGEEEQLRVKEKIGE---LEAEIASLERSIAEKERELEDAEERLAKL------EAEIDKLLAEIEELERE--- 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 293 lSASYEQERKSTSHAINELKEQLNSVVAESESYKSELETVRRKLNNYsdynkiKEELSALKKiefgvNEDDSDNDIRSED 372
Cdd:TIGR02169 345 -IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY------REKLEKLKR-----EINELKRELDRLQ 412
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 373 KNDNTFESSLLSANKKLQATLAEYRSKSTAQEEERNELKKSVDQLKQQIATLKEANEK---LETDLEKVE 439
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQElydLKEEYDRVE 482
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
110-439 |
8.67e-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: 52.38 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 110 SLEKLGKIDDSKELKEKISYLEDKLAKY-ADYETLKSRLLDLEQ--SSAKTLAKRLTAKTQEINSTWEEkgrnWKEREAD 186
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGLkRELSSLQSELRRIENrlDELSQELSDASRKIGEIEKEIEQ----LEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 187 LLKQLTNVQEQNKALEAKISKNIDiegngnedgdqenNQKEVSTRIAEYNLVTQELETTQARIYQ--LEKRNEELSGALA 264
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKS-------------ELKELEARIEELEEDLHKLEEALNDLEArlSHSRIPEIQAELS 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 265 KATSE-AEKETELHAKELKLNQLESENALLsasyEQERKSTSHAINELKEQLNSVVAESESYKSELEtvrrklnnysdyn 343
Cdd:TIGR02169 802 KLEEEvSRIEARLREIEQKLNRLTLEKEYL----EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE------------- 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 344 kikEELSALKKIEFGVNEddsdndirsedkndntfessLLSANKKLQATLAEYRSKSTAQEEERNELKKSVDQLKQQIAT 423
Cdd:TIGR02169 865 ---ELEEELEELEAALRD--------------------LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921
|
330
....*....|....*.
gi 549740 424 LKEANEKLETDLEKVE 439
Cdd:TIGR02169 922 LKAKLEALEEELSEIE 937
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
152-430 |
1.31e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 152 QSSAKTLAKRLTAKTQEINSTweekgrnwKEREADLLKQLTNVQEQNKALEAKISKNidiegngnedgdqennQKEVSTR 231
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAEL--------EKELAALKKEEKALLKQLAALERRIAAL----------------ARRIRAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 232 IAEYNLVTQELETTQARIYQLEKRNEELSGALAKATSEAEKETELHAKELKLNQLESENALLSASYEqerKSTSHAINEL 311
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL---KYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 312 KEQLNSVVAESESYKSELETVRRKLNnysdynKIKEELSALKKiefgvneddsdndirsedkndntfesSLLSANKKLQA 391
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELE------ALLAELEEERA--------------------------ALEALKAERQK 199
|
250 260 270
....*....|....*....|....*....|....*....
gi 549740 392 TLAEYRSKSTAQEEERNELKKSVDQLKQQIATLKEANEK 430
Cdd:COG4942 200 LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
239-440 |
1.51e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.92 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 239 TQELETTQARIYQLEKRNEELSGALAKATSEAEK-ETELHAKELKLNQLESENALLsasyEQERKSTSHAINELKEQLNS 317
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKAlLKQLAALERRIAALARRIRAL----EQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 318 VVAESESYKSELETVRRKLNNYSDYNKIKEELSALKKIEF--------GVNEDDSD--NDIRSEDKNDNTFESSLLSANK 387
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAvrrlqylkYLAPARREqaEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 549740 388 KLQATLAEYRSKSTAQEEERNELKKSVDQLKQQIATLKEANEKLETDLEKVEN 440
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
71-432 |
3.04e-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: 50.83 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 71 QYQREIDNLTQRSKFSEKVLFDVYEKLSEAPDPQPLLQSSLEKLGKIDDSKElkEKISYLEDKLAKYADYETLKSRLLDL 150
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS--RQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 151 EQSSAKTLAKRLTAKTQEINSTWEEKGRNWKEREaDLLKQLTNVQEQNKALEAKISKNIDIEGNGNEDGDQENNQKEVST 230
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIE-ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 231 RIAEYnlVTQELETTQARIyqlEKRNEELSGALAKATSEAEKETELHAK-ELKLNQLESENALLsASYEQERKSTSHAIN 309
Cdd:TIGR02168 831 RRIAA--TERRLEDLEEQI---EELSEDIESLAAEIEELEELIEELESElEALLNERASLEEAL-ALLRSELEELSEELR 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 310 ELKEQLNSVVAESESYKSELETVRRKLNNY-SDYNKIKEELSALKKIEFGVNEddsdndirsEDKNDNTFESSLLSAN-K 387
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLAQLELRLEGLeVRIDNLQERLSEEYSLTLEEAE---------ALENKIEDDEEEARRRlK 975
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 549740 388 KLQATLAEYRSKSTAQEEERNELKKSVDQLKQQIATLKEANEKLE 432
Cdd:TIGR02168 976 RLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
205-440 |
6.33e-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: 49.67 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 205 ISKNIDIEGNGNEDGDQENNQKEVSTRIAEYNLVTQELETTQARIYQLEKRNEELSGALAKATSEAEKETELHAKELKLN 284
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 285 QLESENALLS-ASYEQERKSTSHAINELKEQLNSVVAESESYKSELETVRRKLnnysdyNKIKEELSALkKIEFGVNE-- 361
Cdd:TIGR02168 753 SKELTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL------DELRAELTLL-NEEAANLRer 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 362 -DDSDNDIRSEDKNDNTFESSLLSANK---KLQATLAEYRSKSTAQEEERNELKKSVDQLKQQIATLKEANEKLETDLEK 437
Cdd:TIGR02168 826 lESLERRIAATERRLEDLEEQIEELSEdieSLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
...
gi 549740 438 VEN 440
Cdd:TIGR02168 906 LES 908
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
18-441 |
1.20e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 18 LTNLQRELDADVIEIKDketlsLNSRKSLATETKKFKKLEPEEKLNNVNKI---IKQYQREIDNLTQRSKFSEKVLFDVY 94
Cdd:PRK03918 167 LGEVIKEIKRRIERLEK-----FIKRTENIEELIKEKEKELEEVLREINEIsseLPELREELEKLEKEVKELEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 95 EKLSEAPDPQPLLQSSLEKLGKIDDS-KELKEKISYLEDK------LAKYAD-YETLKSRLLDLEQSSAKtLAKRLTAKT 166
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERiEELKKEIEELEEKvkelkeLKEKAEeYIKLSEFYEEYLDELRE-IEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 167 QEIN---------STWEEKGRNWKEREADLLKQLTNVQEQNKALEAKISKNIDIEG-----NGNEDGDQENNQKEVSTRI 232
Cdd:PRK03918 321 EEINgieerikelEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERlkkrlTGLTPEKLEKELEELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 233 AEynlVTQELETTQARIYQLEKRNEELSGALAKATSeAEKETELHAKELKlnqlESENALLSASYEQERKSTSHAINELK 312
Cdd:PRK03918 401 EE---IEEEISKITARIGELKKEIKELKKAIEELKK-AKGKCPVCGRELT----EEHRKELLEEYTAELKRIEKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 313 EQLNSVVAESESYKSELETVRRKLNNYSDYNKIKEELSALKKIEFgvneddsdndirsedkndntfessllsanKKLQAT 392
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNL-----------------------------EELEKK 523
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 549740 393 LAEYRSkstaQEEERNELKKSVDQLKQQIATLKEANEKLETDLEKVENV 441
Cdd:PRK03918 524 AEEYEK----LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDEL 568
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
121-363 |
1.46e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 121 KELKEKISYLEDKLAKYADYETLKSRLLDLEQssaktLAKRLTAKTQeinstwEEKGRNWKEREADLLKQLTNVQEQNKA 200
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARERLAELEY-----LRAALRLWFA------QRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 201 LEAKIsknidiegngnedgdQENNQKEVSTRIAEYNLVTQELETTQARIYQLEKRNEELSGA---LAKATSEAEKETELH 277
Cdd:COG4913 314 LEARL---------------DALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRrarLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 278 AKELKLNQLESENALlsASYEQERKSTSHAINELKEQLNSVVAESESYKSELETVRRKLNNY-SDYNKIKEELSAlkkiE 356
Cdd:COG4913 379 AEEFAALRAEAAALL--EALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIpARLLALRDALAE----A 452
|
....*..
gi 549740 357 FGVNEDD 363
Cdd:COG4913 453 LGLDEAE 459
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
250-436 |
1.49e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 250 YQLEKRNEELSGALAKATSEAEK-ETELHAKELKLNQLESENALLSASyeQERKSTSHAINELKEQLNSVVAESESYKSE 328
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPElRKELEEAEAALEEFRQKNGLVDLS--EEAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 329 LETVRRKLNNYSDynkikeELSALkkiefgvneddsdndirsedkNDNTFESSLLSANKKLQATLAEYRSKSTAQEEERN 408
Cdd:COG3206 242 LAALRAQLGSGPD------ALPEL---------------------LQSPVIQQLRAQLAELEAELAELSARYTPNHPDVI 294
|
170 180
....*....|....*....|....*....
gi 549740 409 ELKKSVDQLKQQIAT-LKEANEKLETDLE 436
Cdd:COG3206 295 ALRAQIAALRAQLQQeAQRILASLEAELE 323
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
233-430 |
1.75e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 233 AEYNLVTQELETTQ---ARIYQLEKRNEELSGALAKATSE-AEKETELHA-KELKLNQLESENALLS-ASYEQERKSTSH 306
Cdd:PRK11281 56 AEDKLVQQDLEQTLallDKIDRQKEETEQLKQQLAQAPAKlRQAQAELEAlKDDNDEETRETLSTLSlRQLESRLAQTLD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 307 AINELKEQLNSVVAESESYKSELETVRRKLNNYSdynKIKEELSALKKiefgvNEDDSDNDIRSEDKNDNTFESSLLSAN 386
Cdd:PRK11281 136 QLQNAQNDLAEYNSQLVSLQTQPERAQAALYANS---QRLQQIRNLLK-----GGKVGGKALRPSQRVLLQAEQALLNAQ 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 549740 387 KKLQATLAEYRSKSTA-QEEERNELKKSVDQLKQQIATLKEA-NEK 430
Cdd:PRK11281 208 NDLQRKSLEGNTQLQDlLQKQRDYLTARIQRLEHQLQLLQEAiNSK 253
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
182-454 |
3.07e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 182 EREADLLKQL-----TNVQEQNKALEAKISKNIDIEGNGNEDGDQENNQ----KEVSTRIAEYNLVTQELETTQARIYQL 252
Cdd:PRK01156 165 ERNYDKLKDVidmlrAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHsitlKEIERLSIEYNNAMDDYNNLKSALNEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 253 -------EKRNEELSGALAKATSEAEKETELHAKELKLNQLESENALLSASYEQERKSTSHAINELKEQLNSVVAESESY 325
Cdd:PRK01156 245 ssledmkNRYESEIKTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKY 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 326 KSELETVRRKLNNYSDYNKIKEELSALKKIEFGVNEDDSD-----NDIRSEDKNDNTFESSLLSANKKLQATLAEYRSKS 400
Cdd:PRK01156 325 HAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDynsylKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDP 404
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 549740 401 TAQEEERNELKKSVDQLKQQIATLKEANEKLETDLEKVEnvsphfnETASMMSG 454
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELS-------RNMEMLNG 451
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
59-440 |
3.12e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 3.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 59 EEKLNNVNKIIKQYQREIDNLTQRSkfsekvlfdvyEKLSEAPDPQPLLQSSLEKLGKIDDSKELKEKISYLEDKLAKYA 138
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELE-----------EELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 139 D-YETLKSRLLDLE--QSSAKTLAKRLTAKTQEINSTWEEKGRNWKEREADLLKQLTNVQEQNKALEAKISKNIDIEGNG 215
Cdd:COG4717 146 ErLEELEERLEELRelEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 216 NEDGDQENNQKEVST---RIAEYNLV-------------TQELETTQARI--------------YQLEKRNEELSGALAK 265
Cdd:COG4717 226 EEELEQLENELEAAAleeRLKEARLLlliaaallallglGGSLLSLILTIagvlflvlgllallFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 266 ATSEAEKETELHAKELK--------LNQLESENALLSASYEQERKSTSHAINELKEQLNSVVAESESYK-------SELE 330
Cdd:COG4717 306 ELQALPALEELEEEELEellaalglPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllaeagvEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 331 TVRRKLNNYSDYNKIKEELSALKkiefgvneddsdNDIRSEDKndnTFESSLLSANKK-LQATLAEYRSKSTAQEEERNE 409
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELE------------EQLEELLG---ELEELLEALDEEeLEEELEELEEELEELEEELEE 450
|
410 420 430
....*....|....*....|....*....|...
gi 549740 410 LKKSVDQLKQQIATLKEANE--KLETDLEKVEN 440
Cdd:COG4717 451 LREELAELEAELEQLEEDGElaELLQELEELKA 483
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
24-548 |
5.72e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 24 ELDADVIEIKDKETLSLNSRKSLATETKKFKKlepeeKLNNVNKIIKQYQREIDNLTQRSKFSEKVLFDVYEKLSEAPDP 103
Cdd:TIGR04523 100 KLNSDLSKINSEIKNDKEQKNKLEVELNKLEK-----QKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 104 QPLLQSSLEKLGK-IDDSKELKEKISYLEDKLAKY-ADYETLKSRLLDLEQSSaKTLAKRLTAKTQEINSTWEEKGRNWK 181
Cdd:TIGR04523 175 LNLLEKEKLNIQKnIDKIKNKLLKLELLLSNLKKKiQKNKSLESQISELKKQN-NQLKDNIEKKQQEINEKTTEISNTQT 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 182 EreadlLKQLTNvqEQNKALEAKISKNIDIEGNGNEDGDQENNQKEVSTRIAEYNLVTQElETTQARIYQLEKRNEELSG 261
Cdd:TIGR04523 254 Q-----LNQLKD--EQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ-DWNKELKSELKNQEKKLEE 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 262 ALAKATSEAEKETELhakELKLNQLESEnallSASYEQERKSTSHAINELKEQLNSVVAESESYKSELETVRRKLNNYSD 341
Cdd:TIGR04523 326 IQNQISQNNKIISQL---NEQISQLKKE----LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLES 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 342 YNKIKEELSALKkiefgvneddsDNDIRSEDKNDNTFE---SSLLSANKKLQATLAEYRSKSTAQEEERNELKKSVDQLK 418
Cdd:TIGR04523 399 KIQNQEKLNQQK-----------DEQIKKLQQEKELLEkeiERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 419 QQIATLKEANEKLETDLEKVENVSPHFNETASMMSGVTRQMNNRTSHKMSPTSSIIGIPEDGELSGNQ--STILPIVTK- 495
Cdd:TIGR04523 468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEkeSKISDLEDEl 547
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 549740 496 QRDRFRSRNMDLEKQLRQGNSEKGKLKLEISKLKGDNTKLYERIRYLQSYNNN 548
Cdd:TIGR04523 548 NKDDFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKD 600
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
241-437 |
9.82e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 9.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 241 ELETTQARIYQLEKRNEELSGALAKATSE-AEKETELHAKELKLNQLESENALLSASYEQERKstshAINELKEQLNSVV 319
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDElAALEARLEAAKTELEDLEKEIKRLELEIEEVEA----RIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 320 A--ESESYKSELETVRRKLNNYSDynkikEELSALKKIEfgvneddsdndirsedkndntfessllSANKKLQATLAEYR 397
Cdd:COG1579 87 NnkEYEALQKEIESLKRRISDLED-----EILELMERIE---------------------------ELEEELAELEAELA 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 549740 398 SKSTAQEEERNELKKSVDQLKQQIATLKEANEKLETDLEK 437
Cdd:COG1579 135 ELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
16-335 |
1.03e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 16 ADLTNLQRELDADVIEIKDKETLSLNSRKSLATETKKFKKLEPE-----EKLNNVNKIIKQYQREIDNLTQRSKFSEKVL 90
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEieqleQEEEKLKERLEELEEDLSSLEQEIENVKSEL 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 91 FDVYEKLSEAPDPQPLLQSSLEKL-GKIDDS--KELKEKISYLEDKLAKyadyetLKSRLLDLEQ-----SSAKTLAKRL 162
Cdd:TIGR02169 761 KELEARIEELEEDLHKLEEALNDLeARLSHSriPEIQAELSKLEEEVSR------IEARLREIEQklnrlTLEKEYLEKE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 163 TAKTQEINSTWEEKGRNWKEREADLLKQLTNVQEQNKALEAKI----SKNIDIEGNGNE-DGDQENNQKEVSTRIAEYNL 237
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALrdleSRLGDLKKERDElEAQLRELERKIEELEAQIEK 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 238 VTQELETTQARIYQLEKRNEELSGALAKATSEAEKET-------ELHAKELKLNQLESENALLsasyEQERKSTSHAINE 310
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsledvqaELQRVEEEIRALEPVNMLA----IQEYEEVLKRLDE 990
|
330 340
....*....|....*....|....*...
gi 549740 311 LKEQLNSVVAESESYK---SELETVRRK 335
Cdd:TIGR02169 991 LKEKRAKLEEERKAILeriEEYEKKKRE 1018
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
181-330 |
1.27e-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: 44.15 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 181 KEREADLLKQLTNVQEQNKALEAKISK-NIDIEGNGNEDGDQENNQKEVSTRIA-------------EYNLVTQELETTQ 246
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAaKTELEDLEKEIKRLELEIEEVEARIKkyeeqlgnvrnnkEYEALQKEIESLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 247 ARIYQLEKRneelsgalakatsEAEKETELHAKELKLNQLESENALLSASYEQERKSTSHAINELKEQLNSVVAESESYK 326
Cdd:COG1579 103 RRISDLEDE-------------ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
....
gi 549740 327 SELE 330
Cdd:COG1579 170 AKIP 173
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
65-442 |
1.32e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.42 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 65 VNKII----KQYQREIDNLTQRSKFSE-------------KVLFDVYEKLS---------EAPDPQPLLQSSLEKLgkid 118
Cdd:PRK02224 140 VNKLInatpSDRQDMIDDLLQLGKLEEyrerasdarlgveRVLSDQRGSLDqlkaqieekEEKDLHERLNGLESEL---- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 119 dsKELKEKISYLEDKLAKYAD-YETLKSRLLDLEQSSAktlakRLTAKTQEINSTWEEKGRNWKEREaDLLKQLTNVQEQ 197
Cdd:PRK02224 216 --AELDEEIERYEEQREQAREtRDEADEVLEEHEERRE-----ELETLEAEIEDLRETIAETERERE-ELAEEVRDLRER 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 198 NKALEAKISKNIDieGNGNEDGDQENnqkevstriaeynlVTQELETTQARIYQLEKRNEELSGALAKATSEAEKETElh 277
Cdd:PRK02224 288 LEELEEERDDLLA--EAGLDDADAEA--------------VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLRE-- 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 278 akelKLNQLESENALL---SASYEQERKSTSHAINELKEQLNSVVAESESYKSELETVRRKLNNYSDYNK-IKEELSALK 353
Cdd:PRK02224 350 ----DADDLEERAEELreeAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEeLREERDELR 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 354 KiefgvNEDDSDNDIRSEDKNDNTFESsLLSANK-----------KLQATLAEYRSKSTAQEEERNELKKSVDQLKQQIA 422
Cdd:PRK02224 426 E-----REAELEATLRTARERVEEAEA-LLEAGKcpecgqpvegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLE 499
|
410 420
....*....|....*....|...
gi 549740 423 TLKEANE---KLETDLEKVENVS 442
Cdd:PRK02224 500 RAEDLVEaedRIERLEERREDLE 522
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
23-438 |
2.48e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 23 RELDADVIEIKDKETLSLNSRKSLATETKKFKKLEPEEKL-NNVNKIIKQYQREIDNLTQRSKFSEKVLFDVYEKLSEAP 101
Cdd:PRK03918 255 RKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 102 DPQPLLQSSLEKLGKIDDSKE-LKEKISYLEDKLAKYADYETLKSRLLDLEQSSAKTLAKRLTAKTQEIN---STWEEKG 177
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEeLEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEeeiSKITARI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 178 RNWKEREADLLKQLTNV---------------QEQNKALEAKISKNI-DIEGNGNEDGDQENNQKEVSTRIAEYNLVTQE 241
Cdd:PRK03918 415 GELKKEIKELKKAIEELkkakgkcpvcgreltEEHRKELLEEYTAELkRIEKELKEIEEKERKLRKELRELEKVLKKESE 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 242 LETTQARIYQLEKRNEELSGALAKATSEAEKETELHAKEL---------------KLNQLESENALLSASYEQERKSTSH 306
Cdd:PRK03918 495 LIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiklkgeikslkkeleKLEELKKKLAELEKKLDELEEELAE 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 307 AINELKEQLNSVVAESESYKSELETVRRKLNNYSDYNK-IKEELSALKKIEFGVNE-----DDSDNDIRSEDKNDNTFES 380
Cdd:PRK03918 575 LLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKeLEREEKELKKLEEELDKafeelAETEKRLEELRKELEELEK 654
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549740 381 S--------LLSANKKLQATLAEYRSKSTAQEEERNELKKSVDQLKQQIATLKEANEKLEtDLEKV 438
Cdd:PRK03918 655 KyseeeyeeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE-KLEKA 719
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
181-439 |
8.93e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 8.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 181 KEREADLLKQLTNVQEQNKALEAKISKNIDIEGNGNEDGDQENNQKEVSTRIAEYNlvtQELETTQARIYQLEKRNEEL- 259
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERR---ETIEEKRERAEELRERAAELe 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 260 SGALAK--ATSEAEKETELHAKELklnqlesenallsASYEQERKSTSHAINELkEQLNSVVAESESYKSELETVRRKLN 337
Cdd:PRK02224 551 AEAEEKreAAAEAEEEAEEAREEV-------------AELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKRE 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 338 NYSDYN-KIKEELSALKKIEFGVNEDDSDNDIRSEDKNDNTFESSLLSANKKLQATlaeyrskstaqEEERNELKKSVDQ 416
Cdd:PRK02224 617 ALAELNdERRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDEL-----------REERDDLQAEIGA 685
|
250 260
....*....|....*....|...
gi 549740 417 LKQQIATLKEANEKLETDLEKVE 439
Cdd:PRK02224 686 VENELEELEELRERREALENRVE 708
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
173-434 |
1.28e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 173 WEEKGRNWKEREADLLKQLTNVQEQNKALEAKISKNIDIEgngnEDGDQENNQKEVSTRIAEYNLVTQELETTQARIYQL 252
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELR----EELEKLEKLLQLLPLYQELEALEAELAELPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 253 EKRNEELSGA---LAKATSEAEKETELHAKELKLNQLESENALLSASYEQERKSTshAINELKEQLNSVVAESESYKSEL 329
Cdd:COG4717 152 EERLEELRELeeeLEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ--RLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 330 ETVRRKLNNYSDYNKIKEELSALK--------------------------KIEFGVNEDDSDNDIRSEDKNDNTFESSLL 383
Cdd:COG4717 230 EQLENELEAAALEERLKEARLLLLiaaallallglggsllsliltiagvlFLVLGLLALLFLLLAREKASLGKEAEELQA 309
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 549740 384 SA------NKKLQATLAEYRSKSTAQEEERNELKKSVDQLKQQIATLKEANEKLETD 434
Cdd:COG4717 310 LPaleeleEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
95-437 |
1.55e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 95 EKLSEAPDPQPLLQSSLEKLGKIddSKELKEKISYLEDKLAKYADYETL---KSRLLDLEQSSAKTLAKRLTAKTQEIN- 170
Cdd:pfam15921 458 ESLEKVSSLTAQLESTKEMLRKV--VEELTAKKMTLESSERTVSDLTASlqeKERAIEATNAEITKLRSRVDLKLQELQh 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 171 -STWEEKGRNwKEREADLLK-QLTNVQEQNKALEAKISKNIDIEG-NGNEDGDQENNQKEVSTRIAEYNLVTQELETTQ- 246
Cdd:pfam15921 536 lKNEGDHLRN-VQTECEALKlQMAEKDKVIEILRQQIENMTQLVGqHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKd 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 247 ---ARIYQLEKRNEELSGALAK----------ATSEAEKETELHAKELK-----LNQLESENALLSASYEQERKSTSHAI 308
Cdd:pfam15921 615 kkdAKIRELEARVSDLELEKVKlvnagserlrAVKDIKQERDQLLNEVKtsrneLNSLSEDYEVLKRNFRNKSEEMETTT 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 309 NELKEQLNSVvaesesyKSELETVRRKLNNY--SDYNKIKEELSALKKIEFGVNEDDSdndIRSEDKndnTFESSLLSAN 386
Cdd:pfam15921 695 NKLKMQLKSA-------QSELEQTRNTLKSMegSDGHAMKVAMGMQKQITAKRGQIDA---LQSKIQ---FLEEAMTNAN 761
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 549740 387 KKlQATLAEYRSKSTAQ----EEERNELKKSVDQLKQQIATLKEANEKLETDLEK 437
Cdd:pfam15921 762 KE-KHFLKEEKNKLSQElstvATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
107-289 |
1.56e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 107 LQSSLEKLGK------IDDSKELKEKISYLEDKLAKYADYETLKSRLLDLEQsSAKTLAKRLTAKTQEIN--STWEEKGR 178
Cdd:COG4717 51 LEKEADELFKpqgrkpELNLKELKELEEELKEAEEKEEEYAELQEELEELEE-ELEELEAELEELREELEklEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 179 NWKEREAdLLKQLTNVQEQNKALEAKISkniDIEGNGNEDGDQENNQKEVSTRIAEynLVTQELETTQARIYQLEKRNEE 258
Cdd:COG4717 130 LYQELEA-LEAELAELPERLEELEERLE---ELRELEEELEELEAELAELQEELEE--LLEQLSLATEEELQDLAEELEE 203
|
170 180 190
....*....|....*....|....*....|..
gi 549740 259 LSGALAKATSEAEK-ETELHAKELKLNQLESE 289
Cdd:COG4717 204 LQQRLAELEEELEEaQEELEELEEELEQLENE 235
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
218-539 |
1.95e-03 |
|
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: 41.58 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 218 DGDQENNQKEVSTRIAEynlVTQELETTQARIYQLEKRNEELSGALAKATSEAEK-ETELHAKELKLNQLESENALLSAS 296
Cdd:TIGR02168 665 SAKTNSSILERRREIEE---LEEKIEELEEKIAELEKALAELRKELEELEEELEQlRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 297 ---YEQERKSTSHAINELKEQLNSV---VAESESYKSELETVRRKLNnySDYNKIKEELSALKKIEfgvneddsdNDIRS 370
Cdd:TIGR02168 742 veqLEERIAQLSKELTELEAEIEELeerLEEAEEELAEAEAEIEELE--AQIEQLKEELKALREAL---------DELRA 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 371 EDKNDNTFESSLLSANKKLQATLAEYRSKSTAQEEERNELKKSVDQLKQQIATLKEANEKLETDLEKVENVSPHFNEtas 450
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE--- 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 451 mmsgvtrqmnnrtshkmsptssiigipedgelsgnqstilpivtkQRDRFRSRNMDLEKQLRQGNSEKGKLKLEISKLKG 530
Cdd:TIGR02168 888 ---------------------------------------------ALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
....*....
gi 549740 531 DNTKLYERI 539
Cdd:TIGR02168 923 KLAQLELRL 931
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
62-539 |
2.47e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 62 LNNVNKIIKQYQREIDNLTQRSKFSEKVLFDVYEKLSEAP-------DPQPLLQSSLEKLGKIDDSK-----ELKEKISY 129
Cdd:PRK01156 185 IDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSieynnamDDYNNLKSALNELSSLEDMKnryesEIKTAESD 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 130 LEDKLAKYADYETLKSRLLDLEQSSAktlakrlTAKTQEINSTWEEKGR--NWKEREADLLKQLTNVQEQNKALEAKISK 207
Cdd:PRK01156 265 LSMELEKNNYYKELEERHMKIINDPV-------YKNRNYINDYFKYKNDieNKKQILSNIDAEINKYHAIIKKLSVLQKD 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 208 NIDIEGNGNEDGDQENNQKEVSTRIAEYNLVTQELETTQARIYQLEKRNEELSGALAKATSEAEKETELHAKEL-----K 282
Cdd:PRK01156 338 YNDYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELneinvK 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 283 LNQLESENALLSASYEQERKST------------------------SHAINELKEQLNSVVAESESYKSELETVRRKLNN 338
Cdd:PRK01156 418 LQDISSKVSSLNQRIRALRENLdelsrnmemlngqsvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDE 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 339 YSDYNKIKEELSALKKIEFGVNEDDSDNDIRSEDKNDNTFESSLLSANKKLQATLAEYRSKSTAQEEERNE--------- 409
Cdd:PRK01156 498 KIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKRTswlnalavi 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 410 -------LKKSVDQLKQQIATLKEANEKLETDLEKVENVSPHFNETASMMSGVTRQMNNRTSHKMSPTSSIIGIPED--G 480
Cdd:PRK01156 578 slidietNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNykK 657
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 549740 481 ELSGNQSTI--LPIVTKQRDRFRSRNMDLEKQLRQGNSEKGKLKLEISKLKGDNTKLYERI 539
Cdd:PRK01156 658 QIAEIDSIIpdLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRI 718
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
124-349 |
2.59e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 124 KEKISYLEDKLAKYAD-YETLKSRLLDLEQSsAKTLAKRLTAKTQEINSTWEEKgrNWKEREAdllkQLTNVQEQNKALE 202
Cdd:COG4913 609 RAKLAALEAELAELEEeLAEAEERLEALEAE-LDALQERREALQRLAEYSWDEI--DVASAER----EIAELEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 203 AkisknidiegngnEDGDQENNQKEVSTRIAEYNLVTQELETTQARIYQLEKRNE-------ELSGALAKATSEAEKETE 275
Cdd:COG4913 682 A-------------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEqaeeeldELQDRLEAAEDLARLELR 748
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549740 276 LHAKELKLNQLESEN-ALLSASYEQERKSTSHAINELKEQLNSVVAE-SESYKSELETVRRKLNNYSDYNKIKEEL 349
Cdd:COG4913 749 ALLEERFAAALGDAVeRELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLESLPEYLALLDRL 824
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
222-439 |
4.27e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 40.30 E-value: 4.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 222 ENNQKEVSTRIAEYNLV-----TQELETtqARIYQLEKRNEELSGALAKATSEAEKETELHAKELKLNQLESENALLSA- 295
Cdd:PRK05771 15 KSYKDEVLEALHELGVVhiedlKEELSN--ERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 296 ----SYEQERKSTSHAINELKEQLNSVVAESE------------SYKSELETVRRKLNNYSDYNKIKEELSALKKIEFGV 359
Cdd:PRK05771 93 eeleKIEKEIKELEEEISELENEIKELEQEIErlepwgnfdldlSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 360 NEDDSDN------------DIRSEDKnDNTFESSLLSANKKLQATLAEYRSKSTAQEEERNELKKSVDQLKQQIATLK-E 426
Cdd:PRK05771 173 STDKGYVyvvvvvlkelsdEVEEELK-KLGFERLELEEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELlA 251
|
250
....*....|...
gi 549740 427 ANEKLETDLEKVE 439
Cdd:PRK05771 252 LYEYLEIELERAE 264
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
14-169 |
4.29e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.52 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 14 AKADLTNLQRELDADVIEIKDKETLSLNSRKSLATETKKFKKLEpeEKLNNV--NKIIKQYQREIDNLTQRSKFSEKVLF 91
Cdd:COG1579 36 LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE--EQLGNVrnNKEYEALQKEIESLKRRISDLEDEIL 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549740 92 DVYEKLSEAPDPQPLLQSSLEKLgkiddSKELKEKISYLEDKLakyADYETLKSRLLDLEQSSAKTLAKRLTAKTQEI 169
Cdd:COG1579 114 ELMERIEELEEELAELEAELAEL-----EAELEEKKAELDEEL---AELEAELEELEAEREELAAKIPPELLALYERI 183
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
29-437 |
4.91e-03 |
|
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: 39.94 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 29 VIEIKDKETLSLNSRKSLATETKKFKKLEPEEKLNNVNKIIKQYQREIDNLTQRSKFSEKVLFDVY-EKLSEAPDPQPLL 107
Cdd:COG5185 128 SEIVALKDELIKVEKLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISeLKKAEPSGTVNSI 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 108 QSSLEKLGKIDDSKELKEKISYLEDK-LAKYADYETLKSRLLDLEQSSAKTLAKRLTAKTQEINSTwEEKGRNWKEREAD 186
Cdd:COG5185 208 KESETGNLGSESTLLEKAKEIINIEEaLKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGEN-AESSKRLNENANN 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 187 LLKQLTNVQEQNKALEAKISKNIDIEGNGNEDGDQENNQkEVSTRIAEYNLVTQELettQARIYQLEKRNEELSGALAKA 266
Cdd:COG5185 287 LIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQ-ELEESKRETETGIQNL---TAEIEQGQESLTENLEAIKEE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 267 TSEAEKETELHAKELKLNQLESENALLSASYEQERKSTSHAINELKEQLNSVVAESESYKSELETVRRKLNNYSDYNKiK 346
Cdd:COG5185 363 IENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVS-K 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 347 EELSALKKIEFGVNEDDSDNDIRSEDKNDNTFESSllsankklqatlaeyrskstaqEEERNELKKSVDQLKQQIATLKE 426
Cdd:COG5185 442 LLNELISELNKVMREADEESQSRLEEAYDEINRSV----------------------RSKKEDLNEELTQIESRVSTLKA 499
|
410
....*....|.
gi 549740 427 ANEKLETDLEK 437
Cdd:COG5185 500 TLEKLRAKLER 510
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
180-429 |
5.13e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 5.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 180 WKEREADLLKQLTNVQEQNKA------------LEAKISKNID---------IEGNGNEDGDQENNQKEVSTRIAEYNLV 238
Cdd:COG4717 14 FRDRTIEFSPGLNVIYGPNEAgkstllafiramLLERLEKEADelfkpqgrkPELNLKELKELEEELKEAEEKEEEYAEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 239 TQELETTQARIYQLEKRNEELSGALAKAtseaEKETELHAKELKLNQLESENALLSASYEQERKsTSHAINELKEQLNSV 318
Cdd:COG4717 94 QEELEELEEELEELEAELEELREELEKL----EKLLQLLPLYQELEALEAELAELPERLEELEE-RLEELRELEEELEEL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 319 VAESESYKSELETVRRKLNnysdynkikeeLSALKKIEfgvneddsdndirsedkndntfesSLLSANKKLQATLAEYRS 398
Cdd:COG4717 169 EAELAELQEELEELLEQLS-----------LATEEELQ------------------------DLAEELEELQQRLAELEE 213
|
250 260 270
....*....|....*....|....*....|.
gi 549740 399 KSTAQEEERNELKKSVDQLKQQIATLKEANE 429
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
53-438 |
5.53e-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: 40.09 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 53 FKKLEPEEKLNNVNKiikQYQREIDNltqRSKFSEKVLFDVYEKLSEAPDPQPLLQSSLEKLGKIDDSKELKEK--ISYL 130
Cdd:pfam05483 215 FKLKEDHEKIQHLEE---EYKKEIND---KEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDEnlKELI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 131 EDKLAKYADYETLKSRLlDLEQSSAKTLAKRLTAKTQEINSTWEEKGrnwkereadllkqlTNVQEQNKALEAKISKNID 210
Cdd:pfam05483 289 EKKDHLTKELEDIKMSL-QRSMSTQKALEEDLQIATKTICQLTEEKE--------------AQMEELNKAKAAHSFVVTE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 211 IEGNG--------NEDGDQENNQKEVSTRIAEYNLVTQELETTQARIYQLEKRNEELSGALAKATSEAEKETELHAKELK 282
Cdd:pfam05483 354 FEATTcsleellrTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 283 LNQLESENALLSASYEQErkstshaINELKEQLNSVVAESESYKSELETVRRKLNNysdynkikeelSALKKIEFGVNED 362
Cdd:pfam05483 434 LKGKEQELIFLLQAREKE-------IHDLEIQLTAIKTSEEHYLKEVEDLKTELEK-----------EKLKNIELTAHCD 495
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 549740 363 dsdndirsedkndntfesSLLSANKKLQATLAEYRSKSTAQEEERNELKKSVDQLKQQIATLKEANEKLETDLEKV 438
Cdd:pfam05483 496 ------------------KLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESV 553
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
8-432 |
6.69e-03 |
|
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: 39.95 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 8 HALDIWAKADLTNLQRELDADVIEIKDKETLSLNS----RKSLATETKKFKKLEPEEKLNNVNKIIKQYQREIDNLTQRS 83
Cdd:TIGR00618 489 KAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPgpltRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEI 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 84 KFSEKVLFDVYEKLSEAPD----PQPLLQSSLEKLGKIDDSK--ELKEKISYLEDKLAKYadyetlksRLLDLEQSSAKT 157
Cdd:TIGR00618 569 QQSFSILTQCDNRSKEDIPnlqnITVRLQDLTEKLSEAEDMLacEQHALLRKLQPEQDLQ--------DVRLHLQQCSQE 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 158 LAKRLTAKTQ-EINSTWEEKGRNWKEREADLLKQLTNVQEQNKALEAKIsknidiegngnedgDQENNQKEVstrIAEYN 236
Cdd:TIGR00618 641 LALKLTALHAlQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEK--------------EQLTYWKEM---LAQCQ 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 237 LVTQELETtqaRIYQLEKRNEELSGALAKATSEAEKETELHAKELKLNQLESENALLSASYEQERKSTSHAINE-LKEQL 315
Cdd:TIGR00618 704 TLLRELET---HIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALqTGAEL 780
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 316 NSVVAESESYKSELETVRRKLnnysdynkikeelsALKKIEFGVNEDDSDNDIRSEDKNDNTFESSLLSANKKLQATLAE 395
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEDTHLL--------------KTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGE 846
|
410 420 430
....*....|....*....|....*....|....*..
gi 549740 396 YRSkstaQEEERNELKKSVDQLKQQIATLKEANEKLE 432
Cdd:TIGR00618 847 ITH----QLLKYEECSKQLAQLTQEQAKIIQLSDKLN 879
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
65-440 |
7.01e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 39.64 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 65 VNKIIKQYQREIDNLTQRSKFSEKVLFDVYEKLSEAPDPQPLLQSSLEKlgKIDDSKELKEKISYLEDKLAKYADYETLK 144
Cdd:TIGR00606 693 LQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL--KEKEIPELRNKLQKVNRDIQRLKNDIEEQ 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 145 SRLLDL---EQSSAK------TLAKRLTAKTQEINSTWEEKGRNWKEREADLLKQLTN--VQEQNKALEAKISKnidIEG 213
Cdd:TIGR00606 771 ETLLGTimpEEESAKvcltdvTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNqeKQEKQHELDTVVSK---IEL 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 214 NGNEDGDQENNQKEVSTRIAEYNLVTQELETTQARIYQLEKRNEELSGALAKATSE-AEKETELHAKELKLNQLESENAL 292
Cdd:TIGR00606 848 NRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREiKDAKEQDSPLETFLEKDQQEKEE 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 293 LSASYEQERKSTSHAINELKEQLNSVVAESESYKSELE--TVRRKLNNYSDYNKIKEELSALKKIEFGVNED--DSDNDI 368
Cdd:TIGR00606 928 LISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQdgKDDYLKQKETELNTVNAQLEECEKHQEKINEDmrLMRQDI 1007
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549740 369 RSEDKNDNTFESSLlsankklqaTLAEYRSKSTAQEEERNELKKSVDQLkqQIATLKEANEKLETDLEKVEN 440
Cdd:TIGR00606 1008 DTQKIQERWLQDNL---------TLRKRENELKEVEEELKQHLKEMGQM--QVLQMKQEHQKLEENIDLIKR 1068
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
202-444 |
7.59e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 38.94 E-value: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 202 EAKISKNIDIEGNGNEDGDQENNQKEVSTRIAEYN-----LVTQ-----ELETTQARIyqlekRNEELSGALAKATSEAE 271
Cdd:pfam00529 1 LAPLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRVLvkegdRVKAgdvlfQLDPTDYQA-----ALDSAEAQLAKAQAQVA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 272 KeteLHAKELKLNQLESENALLSASYEQerkstshaineLKEQLNSVVAESESYKSELETVRRKLNNYSDYNKIKeelsa 351
Cdd:pfam00529 76 R---LQAELDRLQALESELAISRQDYDG-----------ATAQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIG----- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 352 lkkiefGVNEDDSDNDIRSEDKNDNTFESSllsankklQATLAEYRSKSTAQEEE-RNELKKSVDQLKQQIATLKEANEK 430
Cdd:pfam00529 137 ------GISRESLVTAGALVAQAQANLLAT--------VAQLDQIYVQITQSAAEnQAEVRSELSGAQLQIAEAEAELKL 202
|
250
....*....|....
gi 549740 431 LETDLEKVENVSPH 444
Cdd:pfam00529 203 AKLDLERTEIRAPV 216
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
54-458 |
9.11e-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: 39.39 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 54 KKLEPEEKLNNVNKIIKQYQREIDNLTQRSKFSEKVLFDVYEKLSEAPDPQPLLQssLEKLGKIDDSKELKEKISYLEDK 133
Cdd:pfam01576 69 RKQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQ--LEKVTTEAKIKKLEEDILLLEDQ 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 134 LAKYA-DYETLKSRLLDL------EQSSAKTLAKRLTAKTQEINSTW-----EEKGR-----NWKEREA---DLLKQLTN 193
Cdd:pfam01576 147 NSKLSkERKLLEERISEFtsnlaeEEEKAKSLSKLKNKHEAMISDLEerlkkEEKGRqelekAKRKLEGestDLQEQIAE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 194 VQEQNKALEAKISKNIDIEGNGNEDGDQENNQKevstriaeyNLVTQELETTQARIYQLEKRNEELSGALAKAtseaEKE 273
Cdd:pfam01576 227 LQAQIAELRAQLAKKEEELQAALARLEEETAQK---------NNALKKIRELEAQISELQEDLESERAARNKA----EKQ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 274 TELHAKELKLNQLESENALLSASYEQERKSTSHA-INELKEQLNSvvaESESYKSELETVRRKLNnySDYNKIKEELSAL 352
Cdd:pfam01576 294 RRDLGEELEALKTELEDTLDTTAAQQELRSKREQeVTELKKALEE---ETRSHEAQLQEMRQKHT--QALEELTEQLEQA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 353 KKieFGVNEDDSDNDIRSEDKNDNTFESSLLSAN-------KKLQATLAEYRSKSTAQEEERNELKKSVDQLKQQI---- 421
Cdd:pfam01576 369 KR--NKANLEKAKQALESENAELQAELRTLQQAKqdsehkrKKLEGQLQELQARLSESERQRAELAEKLSKLQSELesvs 446
|
410 420 430
....*....|....*....|....*....|....*..
gi 549740 422 ATLKEANEKLETDLEKVENVSPHFNETASMMSGVTRQ 458
Cdd:pfam01576 447 SLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQ 483
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
108-354 |
9.63e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 39.14 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 108 QSSLEKLGKIddsKELKEKISYLEDKLAKYADYE-TLKSRLLDLEQSSAKTLAKRLTAKTQEInstweekgrnwkEREA- 185
Cdd:PRK05771 39 ELSNERLRKL---RSLLTKLSEALDKLRSYLPKLnPLREEKKKVSVKSLEELIKDVEEELEKI------------EKEIk 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 186 DLLKQLTNVQEQNKALEAKIS-----KNIDIEgngnedgDQENNQKEVSTRIA----EYNLVTQELETTQAriYQLEKRN 256
Cdd:PRK05771 104 ELEEEISELENEIKELEQEIErlepwGNFDLD-------LSLLLGFKYVSVFVgtvpEDKLEELKLESDVE--NVEYIST 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549740 257 EELSGALAkATSEAEKETELhAKELKLNQLESENAllsasyeQERKSTSHAINELKEQLNSVVAESESYKSELETVRRKL 336
Cdd:PRK05771 175 DKGYVYVV-VVVLKELSDEV-EEELKKLGFERLEL-------EEEGTPSELIREIKEELEEIEKERESLLEELKELAKKY 245
|
250
....*....|....*...
gi 549740 337 nnYSDYNKIKEELSALKK 354
Cdd:PRK05771 246 --LEELLALYEYLEIELE 261
|
|
| |
