|
Name |
Accession |
Description |
Interval |
E-value |
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
201-711 |
3.80e-146 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 438.23 E-value: 3.80e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 201 SSRLAQAAESQGAPQSLEAAAQKTGEPQRCINKGLICSNEKEFYTRKLHIDMTPFLKERGSELDSHEEPGGPLRGNAKDS 280
Cdd:pfam15709 3 TSPLTQTTEEQGAQQSLEAAAQKTGEPQSCINKGLICSNRKEFYTRKLHIDMTPFLKDSGEALDSHEEPGEPLGENHQDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 281 QDPELRNKTLACLSTSLAEYNQPSEADTLKSMDG-DYNVHHLHRGPLKREPAFPKKLA----SETPRKKKKRRS-KLLNQ 354
Cdd:pfam15709 83 QDPEPRSVTLSPLSASLGEHIQTPEADTVQNGDGeDYDVHHLHRGLPRHRPESPEKLTavdtSLLPRAREGKTEpRLFNQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 355 KTGVGINHG-KDLVDKAKRKKRTKTHQAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELTPKKEKLGRKMKRTHKERN 433
Cdd:pfam15709 163 ETPASISHAeRELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 434 MEMAAGLSKSDITNSKEAGGTSHQGLLRSHSAAGQ--LSLELDALESQVAIDGRLSSIQATDVASDMECEEERSHEDPSK 511
Cdd:pfam15709 243 LEVAAELSGPDVINSKETEDASERGAFSSDSVVEDpwLSSKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDPSK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 512 ALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQ 591
Cdd:pfam15709 323 ALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 592 QEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQ 671
Cdd:pfam15709 403 QEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQ 482
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1907069567 672 KLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQ 711
Cdd:pfam15709 483 KQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
468-715 |
1.68e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.59 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 468 QLSLELDALESQVA-IDGRLSSIQATDVASDMECEEER-SHEDPSKALQDKKQQE-KASRDRIRIEKAEMRwlKVEQRRR 544
Cdd:COG1196 236 ELEAELEELEAELEeLEAELEELEAELAELEAELEELRlELEELELELEEAQAEEyELLAELARLEQDIAR--LEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 545 EQEELtwlhkEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEI 624
Cdd:COG1196 314 LEERL-----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 625 QRKKQQeaaerAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKL 704
Cdd:COG1196 389 LEALRA-----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250
....*....|.
gi 1907069567 705 AQEQIRQKAAL 715
Cdd:COG1196 464 LLAELLEEAAL 474
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
501-717 |
4.52e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.17 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 501 EEERSHEDPSKAlQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELtwLHKEQLEKAEKMKEELELEQQRRTEENRl 580
Cdd:PTZ00121 1572 AEEDKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK--IKAEELKKAEEEKKKVEQLKKKEAEEKK- 1647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 581 rkqrLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRklQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEM 660
Cdd:PTZ00121 1648 ----KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK--AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907069567 661 --AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLA--LEEATKLAQEQIRQKAALDK 717
Cdd:PTZ00121 1722 kkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAhlKKEEEKKAEEIRKEKEAVIE 1782
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
516-733 |
9.52e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 9.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 516 KKQQEKASR-----DRIRIEKAEMRWLKVEQRRREQEELTwlhKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEerq 590
Cdd:COG1196 206 ERQAEKAERyrelkEELKELEAELLLLKLRELEAELEELE---AELEELEAELEELEAELAELEAELEELRLELEEL--- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 591 qqeeaekkrRLQLQAARERARQQQEELRRKLQEIQRKKQ--QEAAERAEAEKQRQKELEMQLAEEQKRLMEmaEEERLEY 668
Cdd:COG1196 280 ---------ELELEEAQAEEYELLAELARLEQDIARLEErrRELEERLEELEEELAELEEELEELEEELEE--LEEELEE 348
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907069567 669 QQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 733
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
512-733 |
2.36e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 2.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 512 ALQDKKQQEKASRDRIRIEKAEmrwlkvEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQ 591
Cdd:COG1196 231 LLKLRELEAELEELEAELEELE------AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 592 QEEaeKKRRLQLQAARERARQQQEELRRKLQEI-QRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQ 670
Cdd:COG1196 305 ARL--EERRRELEERLEELEEELAELEEELEELeEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907069567 671 QKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 733
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
468-716 |
2.82e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 468 QLSLELDALESQVAiDGRLSSIQATDVASDMECEEERSHEDPSKALQDKK-QQEKASRDRIRIEKAEMRWLKVEQRRREQ 546
Cdd:COG1196 257 ELEAELAELEAELE-ELRLELEELELELEEAQAEEYELLAELARLEQDIArLEERRRELEERLEELEEELAELEEELEEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 547 EELTwlhKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQR 626
Cdd:COG1196 336 EEEL---EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 627 KKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQ 706
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
250
....*....|
gi 1907069567 707 EQIRQKAALD 716
Cdd:COG1196 493 LLLLLEAEAD 502
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
490-717 |
4.06e-11 |
|
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: 66.69 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 490 QATDVASDMECEEERSHEDPSKALQDKKQQ-EKASRDRIRIEKAEMRWLKVEQRRREQEELTWlhKEQLEKAEKMKEELE 568
Cdd:pfam17380 332 QAAIYAEQERMAMERERELERIRQEERKRElERIRQEEIAMEISRMRELERLQMERQQKNERV--RQELEAARKVKILEE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 569 LEQqrRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKlQEIQRKKQQEAAERAEAEKQRQKELEM 648
Cdd:pfam17380 410 ERQ--RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQ-QQVERLRQQEEERKRKKLELEKEKRDR 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 649 QLAEEQKRLM----------EMAEEER--------LEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIR 710
Cdd:pfam17380 487 KRAEEQRRKIlekeleerkqAMIEEERkrkllekeMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERS 566
|
....*..
gi 1907069567 711 QKAALDK 717
Cdd:pfam17380 567 RLEAMER 573
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
601-714 |
6.88e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.83 E-value: 6.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 601 LQLQAARERARQQQEElRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKAR 680
Cdd:PRK09510 92 LQQKQAAEQERLKQLE-KERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKK 170
|
90 100 110
....*....|....*....|....*....|....
gi 1907069567 681 QEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 714
Cdd:PRK09510 171 AEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAE 204
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
511-733 |
9.90e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 9.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 511 KALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKqrleeerq 590
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 591 QQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQR-QKELEMQLAEEQKRLMEMAEEERLEYQ 669
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELeELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907069567 670 QQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 733
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
501-733 |
3.72e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.01 E-value: 3.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 501 EEERSHEDPSKALQDKKQQEKASRDRIR----IEKAEMRwLKVEQRRREQEELTWLHKE-----QLEKAEKMKEELELEQ 571
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKkaeeLKKAEEK-KKAEEAKKAEEDKNMALRKaeeakKAEEARIEEVMKLYEE 1603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 572 QRRTEENRLRKQRLEEERQQQ---EEAEKKRRLQLQAARERARQQQEELRRKLQEIQ------RKKQQEAAERAEAEKQR 642
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEElkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaaeeAKKAEEDKKKAEEAKKA 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 643 QKElEMQLAEEQKRlmeMAEEERLEYQQQKLAAEEKARQE----AEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKH 718
Cdd:PTZ00121 1684 EED-EKKAAEALKK---EAEEAKKAEELKKKEAEEKKKAEelkkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
|
250
....*....|....*
gi 1907069567 719 LHFHQELSKEASGLQ 733
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIR 1774
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
511-702 |
1.80e-09 |
|
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: 61.29 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 511 KALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEqleKAEKMKEELELEQQRRTEENRLRKQRLEEERQ 590
Cdd:pfam17380 399 EAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEE---RAREMERVRLEEQERQQQVERLRQQEEERKRK 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 591 QQEEAEKKRRLQLQAARERA--RQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEY 668
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKilEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907069567 669 QQQKLAAEEKARQEAEERRKQ------EEEAAKLALEEAT 702
Cdd:pfam17380 556 EQMRKATEERSRLEAMEREREmmrqivESEKARAEYEATT 595
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
501-728 |
2.20e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.31 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 501 EEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLhkEQLEKAEKMKEELELEQQRRTEENRL 580
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV--EQLKKKEAEEKKKAEELKKAEEENKI 1661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 581 RKqrleeerqqqeEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraeaeKQRQKELEMQLAEEQKRlmem 660
Cdd:PTZ00121 1662 KA-----------AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE---------AKKAEELKKKEAEEKKK---- 1717
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069567 661 AEEERLEYQQQKLAAEEKARQEAEERRKQEEeaAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKE 728
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAEE--AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
605-729 |
2.48e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.82 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 605 AARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQ-----RQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKA 679
Cdd:PRK09510 60 VVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQaaeqeRLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1907069567 680 RQEAEERRKQEEEAAKLAleEATKLAQEQIRQKAALDKHLHFHQELSKEA 729
Cdd:PRK09510 140 KAAAAAKAKAEAEAKRAA--AAAKKAAAEAKKKAEAEAAKKAAAEAKKKA 187
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
597-717 |
4.79e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 58.70 E-value: 4.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 597 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEyQQQKLAAE 676
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE-AKAKQAAE 131
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1907069567 677 EKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDK 717
Cdd:TIGR02794 132 AKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAK 172
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
501-713 |
6.09e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 6.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 501 EEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENR- 579
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKk 1553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 580 ---LRKQRLEEERQQQEEAEKKRRLQLQAARE--RARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMqlAEEQ 654
Cdd:PTZ00121 1554 aeeLKKAEEKKKAEEAKKAEEDKNMALRKAEEakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK--AEEE 1631
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 655 KRLMEM-----------AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKlalEEATKLAQEQIRQKA 713
Cdd:PTZ00121 1632 KKKVEQlkkkeaeekkkAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA---EEDEKKAAEALKKEA 1698
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
501-717 |
6.80e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 6.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 501 EEERSHEDPSKAlQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQL----EKAEKMKEELELEQQRRTE 576
Cdd:PTZ00121 1215 EEARKAEDAKKA-EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaikaEEARKADELKKAEEKKKAD 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 577 ENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQE------IQRKKQQEAAERAEAEKQRQKELEMQL 650
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEakkaaeAAKAEAEAAADEAEAAEEKAEAAEKKK 1373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 651 AEEQKR---LMEMAEEERLEYQQQKLAAEEKarQEAEERRKQEEEAAKlaLEEATKLAQEQIRQKAALDK 717
Cdd:PTZ00121 1374 EEAKKKadaAKKKAEEKKKADEAKKKAEEDK--KKADELKKAAAAKKK--ADEAKKKAEEKKKADEAKKK 1439
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
498-717 |
1.53e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.15 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 498 MECEEERSHEDPSKALQDKKQQEKASRDRIRieKAEMRWLKVEQRRREQEEltwlhKEQLEKAEKMKEELELEQQRRTEE 577
Cdd:PTZ00121 1272 IKAEEARKADELKKAEEKKKADEAKKAEEKK--KADEAKKKAEEAKKADEA-----KKKAEEAKKKADAAKKKAEEAKKA 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 578 NRLRKQRLEEERQQQEEAEKKRRLQlQAARERARQQQEELRRKLQEIqrKKQQEAAERAEAEKQRQKELEMQLAEEQK-- 655
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEAA-EKKKEEAKKKADAAKKKAEEK--KKADEAKKKAEEDKKKADELKKAAAAKKKad 1421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907069567 656 RLMEMAEEERLEYQQQKLAAE----EKARQEAEERRKQEE-----EAAKLAlEEATKLAQEQIRQKAALDK 717
Cdd:PTZ00121 1422 EAKKKAEEKKKADEAKKKAEEakkaDEAKKKAEEAKKAEEakkkaEEAKKA-DEAKKKAEEAKKADEAKKK 1491
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
380-727 |
2.12e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 2.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 380 QAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELTPKKEKLGRKMKRTHKERNMEMAAGLSKSDITNSKEAGGTSHQGL 459
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 460 LRSHSAAGQLSLELDALESQVAIDGRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKV 539
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 540 EQRRREQEELTwlhKEQLEKAEKMKEELELEQQRRTEENRLR---KQRLEEERQQQEEAEKKRRLQLQAARERarqQQEE 616
Cdd:PTZ00121 1401 EEDKKKADELK---KAAAAKKKADEAKKKAEEKKKADEAKKKaeeAKKADEAKKKAEEAKKAEEAKKKAEEAK---KADE 1474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 617 LRRKLQEIQRK---KQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKarQEAEERRKQEE-- 691
Cdd:PTZ00121 1475 AKKKAEEAKKAdeaKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA--KKAEEKKKADElk 1552
|
330 340 350
....*....|....*....|....*....|....*.
gi 1907069567 692 EAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSK 727
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
511-708 |
2.65e-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: 54.29 E-value: 2.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 511 KALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHK-EQLEKAEKMKEELELEQQRRTEENRLRKQRLEEER 589
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 590 QQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRK--KQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEerLE 667
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAE--IE 862
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907069567 668 YQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQ 708
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
604-729 |
3.49e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.93 E-value: 3.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 604 QAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRlmemAEEERLEYQQQKLAAEEKARQEA 683
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAA----AEKAAKQAEQAAKQAEEKQKQAE 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1907069567 684 EERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEA 729
Cdd:TIGR02794 123 EAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKA 168
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
469-747 |
4.60e-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: 53.53 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 469 LSLELDALESQ-VAIDGRLSSIQA--TDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQR--R 543
Cdd:TIGR02169 228 LLKEKEALERQkEAIERQLASLEEelEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAslE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 544 REQEELtwlhKEQLEKAEKmkeeleleQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQE 623
Cdd:TIGR02169 308 RSIAEK----ERELEDAEE--------RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 624 IQRKKQqeaaERAEAEKQRQKELEM------QLAEEQKRLMEMAE---------EERLEYQQQKLAAEEKARQEAEERRK 688
Cdd:TIGR02169 376 VDKEFA----ETRDELKDYREKLEKlkreinELKRELDRLQEELQrlseeladlNAAIAGIEAKINELEEEKEDKALEIK 451
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069567 689 QEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQWTQNISRPWVYSYF 747
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
511-711 |
7.02e-07 |
|
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: 52.82 E-value: 7.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 511 KALQDKKQQEKASR---DRIRIEKAEmRWLKVEQRRR--------------------EQEELTWLHKEQLEKAEKMKEEL 567
Cdd:pfam17380 282 KAVSERQQQEKFEKmeqERLRQEKEE-KAREVERRRKleeaekarqaemdrqaaiyaEQERMAMERERELERIRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 568 ELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRL--QLQAAReRARQQQEELRRKLQEIQRKKQQeaaERAEAEKQRQKE 645
Cdd:pfam17380 361 ELERIRQEEIAMEISRMRELERLQMERQQKNERVrqELEAAR-KVKILEEERQRKIQQQKVEMEQ---IRAEQEEARQRE 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069567 646 LEmQLAEEQKRLMEMAEEERLEYQQQKlaaeEKARQEAEERRKQEEEAAKlaLEEATKLAQEQIRQ 711
Cdd:pfam17380 437 VR-RLEEERAREMERVRLEEQERQQQV----ERLRQQEEERKRKKLELEK--EKRDRKRAEEQRRK 495
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
604-714 |
9.60e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.80 E-value: 9.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 604 QAARERARQQQEELRRklQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLmEMAEEERLEyQQQKLAAEEKARQEA 683
Cdd:COG2268 241 EAEAELAKKKAEERRE--AETARAEAEAAYEIAEANAEREVQRQLEIAEREREI-ELQEKEAER-EEAELEADVRKPAEA 316
|
90 100 110
....*....|....*....|....*....|..
gi 1907069567 684 EERRKQEEEAAKLALEEATKLAQ-EQIRQKAA 714
Cdd:COG2268 317 EKQAAEAEAEAEAEAIRAKGLAEaEGKRALAE 348
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
574-729 |
3.37e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 574 RTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQ-EAAERAEAEKQRQKELEMQLAE 652
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069567 653 EQKRLMEMaeEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEA 729
Cdd:COG4717 144 LPERLEEL--EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
457-707 |
4.91e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 457 QGLLRSHSAAGQLSLELDALESQVAidgRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRdRIRIEKAEMRW 536
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELA---ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA-LLEAEAELAEA 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 537 LKVEQRRREQEEltwlhkeQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEE 616
Cdd:COG1196 378 EEELEELAEELL-------EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 617 LRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKL 696
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
|
250
....*....|.
gi 1907069567 697 ALEEATKLAQE 707
Cdd:COG1196 531 GVEAAYEAALE 541
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
507-717 |
9.83e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 48.72 E-value: 9.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 507 EDPSKAL--QDKKQQEKASRDRiRIEKAEMRW---LKVEQRRREQEEltwlhkEQLEKAEKMKEELELEQQRRTEEnrlr 581
Cdd:COG2268 180 EDENNYLdaLGRRKIAEIIRDA-RIAEAEAEReteIAIAQANREAEE------AELEQEREIETARIAEAEAELAK---- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 582 kqrleeerqqqeeaeKKRRLQLQAARERARQQQE-ELRR--KLQEIQRKKQQEaaeraeaekQRQKELEMQLAEEQKRLM 658
Cdd:COG2268 249 ---------------KKAEERREAETARAEAEAAyEIAEanAEREVQRQLEIA---------EREREIELQEKEAEREEA 304
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907069567 659 EMAEEERLEYQQQKLAAEEKARQEAE-ERRKQEEEA-AKLALEEATKLAQEQIRQKAALDK 717
Cdd:COG2268 305 ELEADVRKPAEAEKQAAEAEAEAEAEaIRAKGLAEAeGKRALAEAWNKLGDAAILLMLIEK 365
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
597-707 |
1.17e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 597 KKRRLQLQAARERARQQQEELRRKLQEIQRK------KQQEAAERAEAEKQRQKELEMQLAEEQKRL------------- 657
Cdd:PRK12704 78 RERRNELQKLEKRLLQKEENLDRKLELLEKReeelekKEKELEQKQQELEKKEEELEELIEEQLQELerisgltaeeake 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1907069567 658 --MEMAEEErleyqqqklaaeekARQEAEERRKQEEEAAKlalEEATKLAQE 707
Cdd:PRK12704 158 ilLEKVEEE--------------ARHEAAVLIKEIEEEAK---EEADKKAKE 192
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
597-723 |
1.71e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 597 KKRRLQLQAARERARQQQE-ELRRKLQEIQRKKQQEaaeraeaeKQRQKELEMQLAEEQKRlmemaeEERLEYQQQKLAA 675
Cdd:PRK12704 56 KEALLEAKEEIHKLRNEFEkELRERRNELQKLEKRL--------LQKEENLDRKLELLEKR------EEELEKKEKELEQ 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069567 676 E----EKARQEAEERRKQE----EEAAKLALEEATKLAQEQIRQKAALDKHLHFHQ 723
Cdd:PRK12704 122 KqqelEKKEEELEELIEEQlqelERISGLTAEEAKEILLEKVEEEARHEAAVLIKE 177
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
514-714 |
1.86e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.94 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 514 QDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQE 593
Cdd:pfam02029 143 NKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVT 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 594 EAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRlmemAEEERleyqqqkl 673
Cdd:pfam02029 223 TKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKK----REERR-------- 290
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1907069567 674 aaeeKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 714
Cdd:pfam02029 291 ----KLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERRRA 327
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
516-715 |
2.13e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 516 KKQQEKASRDRIRIEKAEmrwLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEA 595
Cdd:COG4717 60 KPQGRKPELNLKELKELE---EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEA 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 596 EKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaerAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAA 675
Cdd:COG4717 137 LEAELAELPERLEELEERLEELRELEEELEELEAE-----LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1907069567 676 EEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAAL 715
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
511-721 |
2.32e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 511 KALQDKKQQEKASRDRIR--IEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEE--NRLRKQRLE 586
Cdd:COG4942 37 AELEKELAALKKEEKALLkqLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElaELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 587 EERQQQE-------EAEKKRRLQLQAARERARQQQ-EELRRKLQEIQRKKQQeaaerAEAEKQRQKELEMQLAEEQKRLm 658
Cdd:COG4942 117 GRQPPLAlllspedFLDAVRRLQYLKYLAPARREQaEELRADLAELAALRAE-----LEAERAELEALLAELEEERAAL- 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907069567 659 emaeeERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHF 721
Cdd:COG4942 191 -----EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
499-684 |
2.47e-05 |
|
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: 47.81 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 499 ECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKaekmkeeLELEQQRRTEEN 578
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEK-------EKRDRKRAEEQR 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 579 R-LRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraEAEKQRQKELEMQLAEEQKRL 657
Cdd:pfam17380 494 RkILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQ------EMEERRRIQEQMRKATEERSR 567
|
170 180
....*....|....*....|....*..
gi 1907069567 658 MEMAEEERLEYQQqkLAAEEKARQEAE 684
Cdd:pfam17380 568 LEAMEREREMMRQ--IVESEKARAEYE 592
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
597-717 |
3.50e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 47.01 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 597 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAE-----EERLEYQQQ 671
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEkldnlENQLEEREK 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1907069567 672 KLAAEEKARQEAEERRKQE-EEAAKLALEEATKLAQEQIRQKAALDK 717
Cdd:PRK12705 113 ALSARELELEELEKQLDNElYRVAGLTPEQARKLLLKLLDAELEEEK 159
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
501-705 |
3.78e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 501 EEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRwlkvEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRL 580
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELE----EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 581 RKQRLEEERQQQEEAEKKRRL-----QLQAARERARQQQEELRRKLQEIQRKKQQEA----AERAEAEKQRQKELEMQLA 651
Cdd:TIGR02168 385 RSKVAQLELQIASLNNEIERLearleRLEDRRERLQQEIEELLKKLEEAELKELQAEleelEEELEELQEELERLEEALE 464
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1907069567 652 EEQKRLMEMAEEER-LEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLA 705
Cdd:TIGR02168 465 ELREELEEAEQALDaAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
501-710 |
5.08e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 501 EEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEEltwlHKEQLE-KAEKMKEELELEQQRRTEENR 579
Cdd:TIGR02169 204 RREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE----ELEKLTeEISELEKRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 580 lrkqRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeAAERAEAEKQRQKELEMQLAEEQKRLME 659
Cdd:TIGR02169 280 ----KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK-LEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069567 660 MAEE-----ERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIR 710
Cdd:TIGR02169 355 LTEEyaelkEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
501-698 |
5.10e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 501 EEERSHEDPSKALQDKKQQEKASRDRIRIEKAEmrwLKVEQRRREQEELTWLHKEQLEKAEkmkeeleleQQRRTEENRL 580
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEE---LREELEKLEKLLQLLPLYQELEALE---------AELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 581 RKQRLEEerqqqeeaekKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEm 660
Cdd:COG4717 149 EELEERL----------EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE- 217
|
170 180 190
....*....|....*....|....*....|....*...
gi 1907069567 661 aEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLAL 698
Cdd:COG4717 218 -AQEELEELEEELEQLENELEAAALEERLKEARLLLLI 254
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
571-719 |
5.21e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 46.53 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 571 QQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQL 650
Cdd:pfam05262 204 KERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREI 283
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069567 651 AEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLaQEQIRQKAALDKHL 719
Cdd:pfam05262 284 EKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDL-QKTKPQVEAQPTSL 351
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
540-717 |
6.51e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.99 E-value: 6.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 540 EQRRREQEELtwlhkEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRR 619
Cdd:TIGR02794 61 PAAKKEQERQ-----KKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 620 KLQEIQRKKQQEAaeraeaEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEaEERRKQEEEAAKLALE 699
Cdd:TIGR02794 136 AEAEAERKAKEEA------AKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAE-EAKAKAEAAKAKAAAE 208
|
170
....*....|....*...
gi 1907069567 700 EATKLAQEQIRQKAALDK 717
Cdd:TIGR02794 209 AAAKAEAEAAAAAAAEAE 226
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
602-726 |
6.74e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.59 E-value: 6.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 602 QLQAARERAR----------QQQEELRRKLQEIQRKKQ----------QEAAERAEAEKQRQK----ELEM-QL-AEEQK 655
Cdd:PRK10929 124 QAQQEQDRAReisdslsqlpQQQTEARRQLNEIERRLQtlgtpntplaQAQLTALQAESAALKalvdELELaQLsANNRQ 203
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069567 656 RLMEMAEE------ERLEYQQQKLaaeekaRQEAEERRKQEeeaAKLALEEATKLAQEQIRQKAALDKHLHFHQELS 726
Cdd:PRK10929 204 ELARLRSElakkrsQQLDAYLQAL------RNQLNSQRQRE---AERALESTELLAEQSGDLPKSIVAQFKINRELS 271
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
516-715 |
7.60e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.20 E-value: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 516 KKQQEKASRDR-IRIEKAEMRW----LKVEQRRREQEELtwlhKEQLEKAEKMKEELELEQQRRTEE-NRLRKQrleeer 589
Cdd:TIGR02168 206 ERQAEKAERYKeLKAELRELELallvLRLEELREELEEL----QEELKEAEEELEELTAELQELEEKlEELRLE------ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 590 qqqEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraeaEKQRQKELEMQLAEEQKRLMEMAEE-ERLEY 668
Cdd:TIGR02168 276 ---VSELEEEIEELQKELYALANEISRLEQQKQILRERLAN--------LERQLEELEAQLEELESKLDELAEElAELEE 344
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1907069567 669 QQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAAL 715
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
540-717 |
9.90e-05 |
|
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: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 540 EQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQL--QAARERARQQQEEL 617
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLdyLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 618 RRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLA 697
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180
....*....|....*....|
gi 1907069567 698 LEEATKLAQEQIRQKAALDK 717
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELK 345
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
597-728 |
1.86e-04 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 44.84 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 597 KKRRLQLQAARerarQQQEELRRKL-----------QEIQRKKQ-----QEAAERAEAEKQRQKE--------------- 645
Cdd:pfam09726 405 KKLKAELQASR----QTEQELRSQIssltslerslkSELGQLRQendllQTKLHNAVSAKQKDKQtvqqlekrlkaeqea 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 646 ---LEMQLAEEQKRLMEmaEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFH 722
Cdd:pfam09726 481 rasAEKQLAEEKKRKKE--EEATAARAVALAAASRGECTESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQELRKY 558
|
....*.
gi 1907069567 723 QELSKE 728
Cdd:pfam09726 559 KESEKD 564
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
538-714 |
1.93e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.41 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 538 KVEQRRREQEEltwlhKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEEL 617
Cdd:PRK09510 71 QKSAKRAEEQR-----KKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 618 RRKlQEIQRKKQQEAAERAEAEKQRQKElemqlAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLA 697
Cdd:PRK09510 146 KAK-AEAEAKRAAAAAKKAAAEAKKKAE-----AEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKA 219
|
170
....*....|....*..
gi 1907069567 698 LEEATKLAQEQIRQKAA 714
Cdd:PRK09510 220 AAEAKAAAAKAAAEAKA 236
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
503-714 |
2.63e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 503 ERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRK 582
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 583 qrleeerqqqeeaekkRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEM------QLAEEQKR 656
Cdd:pfam13868 188 ----------------RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELqqareeQIELKERR 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069567 657 LMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLAlEEATKLAQEQIRQKAA 714
Cdd:pfam13868 252 LAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHR-RELEKQIEEREEQRAA 308
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
602-714 |
2.82e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 602 QLQAARERARQQQEELRRKLQEIQRKKQQEaaeraeaeKQRQKELEMQLAEEQKRLMEMAEEERlEYQQQKlAAEEKARQ 681
Cdd:COG3883 137 ELKADKAELEAKKAELEAKLAELEALKAEL--------EAAKAELEAQQAEQEALLAQLSAEEA-AAEAQL-AELEAELA 206
|
90 100 110
....*....|....*....|....*....|...
gi 1907069567 682 EAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 714
Cdd:COG3883 207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
517-728 |
2.87e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 517 KQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRrtEENRLRKQRLEEERQQQEEAE 596
Cdd:pfam13868 26 AQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQI--EEREQKRQEEYEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 597 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAE-----EQKRLMEMAEEERLEYQQQ 671
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEylkekAEREEEREAEREEIEEEKE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907069567 672 KLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKE 728
Cdd:pfam13868 184 REIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQA 240
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
518-728 |
3.05e-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: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 518 QQEKASRDRIRIEKAEmrwlKVEQRRREQEeltwlhKEQLEKaekmkeelelEQQRRTEENRLRKQRLEEERQQQEEAEK 597
Cdd:pfam17380 279 QHQKAVSERQQQEKFE----KMEQERLRQE------KEEKAR----------EVERRRKLEEAEKARQAEMDRQAAIYAE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 598 KRRLQLQAARERARQQQEELRRKLQEI----------------------QRKKQQEAAERAEAEKQRQKELEMQ-LAEEQ 654
Cdd:pfam17380 339 QERMAMERERELERIRQEERKRELERIrqeeiameisrmrelerlqmerQQKNERVRQELEAARKVKILEEERQrKIQQQ 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907069567 655 KRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKE 728
Cdd:pfam17380 419 KVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ 492
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
520-733 |
3.19e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 520 EKASRDRIRIEKAEMRWLK-----VEQRRREQEELTWL--HKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQ 592
Cdd:COG4913 220 EPDTFEAADALVEHFDDLEraheaLEDAREQIELLEPIreLAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 593 EEAEKKRrlqLQAARERARQQQEELRRKLQEIQRKKQQEAAeraeaekQRQKELEMQLAEEQKRLMEmAEEERLEYQQQK 672
Cdd:COG4913 300 LRAELAR---LEAELERLEARLDALREELDELEAQIRGNGG-------DRLEQLEREIERLERELEE-RERRRARLEALL 368
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907069567 673 LAAEEKARQEAEE--RRKQEEEAAKLALEEATKLAQEQIRQ-KAALDKHLHFHQELSKEASGLQ 733
Cdd:COG4913 369 AALGLPLPASAEEfaALRAEAAALLEALEEELEALEEALAEaEAALRDLRRELRELEAEIASLE 432
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
380-711 |
3.27e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 380 QAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELtpkKEKLGRKMKRTHKERNMEMAAGLSKSDITNSKEAGGTshQGL 459
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAEL---LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL--RGL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 460 LRSHSAAGQLSLELDALEsQVAIDGRLSSIQATDVASDMECEEERSHEDPSKA----LQDKKQQEKASRDRIRIEKAEMR 535
Cdd:COG1196 523 AGAVAVLIGVEAAYEAAL-EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflpLDKIRARAALAAALARGAIGAAV 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 536 WLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLR-KQRLEEERQQQEEAEKKRRLQLQAARERARQQQ 614
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLReVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 615 EELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAA 694
Cdd:COG1196 682 EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPD 761
|
330
....*....|....*..
gi 1907069567 695 KLALEEATKLAQEQIRQ 711
Cdd:COG1196 762 LEELERELERLEREIEA 778
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
608-692 |
4.20e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 41.56 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 608 ERARQQQEELRRKLQEiQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEY-QQQKLAAEEKARQEAEER 686
Cdd:pfam05672 39 EEERLRKEELRRRAEE-ERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERlQKQKEEAEAKAREEAERQ 117
|
....*.
gi 1907069567 687 RKQEEE 692
Cdd:pfam05672 118 RQEREK 123
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
456-737 |
4.93e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 4.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 456 HQGLLRSHSAAGQLSLELDALESQV-AIDGRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQekasrdRIRIEKAEM 534
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELqELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ------QKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 535 RWLKVEQRRREqeeltwlhkEQLEKAEkmkeELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQ 614
Cdd:TIGR02168 312 ANLERQLEELE---------AQLEELE----SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 615 EELRRKLQEIQRKKQQEAAERAeaekqRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAA 694
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNN-----EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ 453
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1907069567 695 K--LALEEATKLAQEQIRQK-AALDKHLHFHQELSKEASGLQWTQN 737
Cdd:TIGR02168 454 EelERLEEALEELREELEEAeQALDAAERELAQLQARLDSLERLQE 499
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
516-740 |
6.29e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 43.29 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 516 KKQQEKASRDRIRIEKAEMRWLK-----VEQRRREQEELTwLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQ 590
Cdd:pfam12128 311 SAADAAVAKDRSELEALEDQHGAfldadIETAAADQEQLP-SWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNN 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 591 QQEEAEKKRRlqlQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLME-MAEEERLEYQ 669
Cdd:pfam12128 390 RDIAGIKDKL---AKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQaTATPELLLQL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 670 QQKLAAEEKARQEAEERRKQ------EEEAAKLALEEAT-KLAQEQIR---QKAALDKHLH--------FHQELSKEASG 731
Cdd:pfam12128 467 ENFDERIERAREEQEAANAEverlqsELRQARKRRDQASeALRQASRRleeRQSALDELELqlfpqagtLLHFLRKEAPD 546
|
....*....
gi 1907069567 732 lqWTQNISR 740
Cdd:pfam12128 547 --WEQSIGK 553
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
486-728 |
7.37e-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: 43.04 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 486 LSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKV-EQRRREQEELTWLHKEQLEKAEKMK 564
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERrKVDDEEKLKESEKEKKKAEKELKKE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 565 EELELEQQRRTEENRLRKQRLEEERQQqeeaekkrrlqlqaarerARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQK 644
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAEEEEEEE------------------LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 645 ELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEaAKLALEEATKLAQEQIRQKAALDKHLHFHQE 724
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ-GKLTEEKEELEKQELKLLKDELELKKSEDLL 474
|
....
gi 1907069567 725 LSKE 728
Cdd:pfam02463 475 KETQ 478
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
591-695 |
7.39e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 591 QQEEAEKKRRLQLQAARERARQQQEELRRKLQEiQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEM-AEEERLEYQ 669
Cdd:PRK11637 170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYE-QQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELrANESRLRDS 248
|
90 100 110
....*....|....*....|....*....|.
gi 1907069567 670 QQKLAAEEKARQEAEER-----RKQEEEAAK 695
Cdd:PRK11637 249 IARAEREAKARAEREAReaarvRDKQKQAKR 279
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
530-700 |
7.99e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.21 E-value: 7.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 530 EKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQeeaeKKRRLQLQAARER 609
Cdd:pfam13868 166 EREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE----KKARQRQELQQAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 610 ARQQQEELRRKLQEIQR---------KKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKAR 680
Cdd:pfam13868 242 EEQIELKERRLAEEAEReeeefermlRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLR 321
|
170 180
....*....|....*....|
gi 1907069567 681 QEAEERRKQEEEAAKLALEE 700
Cdd:pfam13868 322 EEEAERRERIEEERQKKLKE 341
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
615-717 |
8.38e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 615 EELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMaeEERLEYQQQKLAAEEKARQEAEERRKQEEEaa 694
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEAL--KARWEAEKELIEEIQELKEELEQRYGKIPE-- 489
|
90 100
....*....|....*....|...
gi 1907069567 695 klaLEEATKLAQEQIRQKAALDK 717
Cdd:COG0542 490 ---LEKELAELEEELAELAPLLR 509
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
514-705 |
1.03e-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: 42.65 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 514 QDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEEltWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQE 593
Cdd:TIGR00618 208 LCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH--AYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQER 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 594 EAEKKRRLQL---QAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQkrLMEMAEEERLEYQQ 670
Cdd:TIGR00618 286 INRARKAAPLaahIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT--LHSQEIHIRDAHEV 363
|
170 180 190
....*....|....*....|....*....|....*
gi 1907069567 671 QKLAAEEKARQEAEERRKQEEEAAKLALEEATKLA 705
Cdd:TIGR00618 364 ATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSL 398
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
640-714 |
1.09e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 39.73 E-value: 1.09e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069567 640 KQRQKELEMQLAEEQKRLMEM---AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 714
Cdd:cd06503 43 EKAKEEAEELLAEYEEKLAEAraeAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVA 120
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
379-713 |
1.15e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 379 HQAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELTPKKEKLGRKMKRTHKERNMEMAAGLSKSDITNSKEAGGTSHQG 458
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 459 LLRSHSAAGQLSLELDALESQVAIDGRLSSIQATDVASDMECEEE----------RSHEDPSKALQDKKQQEKASRDRIR 528
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaaalqnivvEDDEVAAAAIEYLKAAKAGRATFLP 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 529 IEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARE 608
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 609 RARQQQEELRRKLQEIQRKKQQEAAE--RAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEER 686
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELaeRLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
330 340
....*....|....*....|....*..
gi 1907069567 687 RKQEEEAAKLALEEATKLAQEQIRQKA 713
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEEL 765
|
|
| DDRGK |
pfam09756 |
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ... |
619-693 |
1.16e-03 |
|
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and vertebrates. They contain a highly conserved DDRGK motif.
Pssm-ID: 370664 [Multi-domain] Cd Length: 188 Bit Score: 40.79 E-value: 1.16e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907069567 619 RKLQEIQRKKQQEAAEraeaeKQRQKELEMQLAEEQKRLMEMAEEERLEYQ----QQKLAAEEKARQEAEERRKQEEEA 693
Cdd:pfam09756 1 KKLGAKKRAKLELKEA-----KRQQREAEEEEREEREKLEEKREEEYKEREereeEAEKEKEEEERKQEEEQERKEQEE 74
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
499-729 |
1.27e-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: 42.27 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 499 ECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEEN 578
Cdd:pfam02463 195 LKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKEN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 579 RLRKQRLEEERQQQEEAEKKRRlQLQAARERARQQQEELRRKLQEIQR---------KKQQEAAERAEAEKQRQ--KELE 647
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEE-ELKSELLKLERRKVDDEEKLKESEKekkkaekelKKEKEEIEELEKELKELeiKREA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 648 MQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRkqEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSK 727
Cdd:pfam02463 354 EEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK--EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEI 431
|
..
gi 1907069567 728 EA 729
Cdd:pfam02463 432 LE 433
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
468-702 |
1.62e-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: 41.88 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 468 QLSLELDALESQVaidgrLSSIQATDVASDMECEEERSHEDPSKaLQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQE 547
Cdd:pfam02463 268 AQVLKENKEEEKE-----KKLQEEELKLLAKEEEELKSELLKLE-RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 548 ELTWLHKEQLEKAEKMKEEleLEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAAR----ERARQQQEELRRKLQE 623
Cdd:pfam02463 342 KELKELEIKREAEEEEEEE--LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELkseeEKEAQLLLELARQLED 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 624 IQRKKQQEAAERAEAEKQRQKELEMQLAEEQ-KRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEAT 702
Cdd:pfam02463 420 LLKEEKKEELEILEEEEESIELKQGKLTEEKeELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERS 499
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
597-698 |
2.58e-03 |
|
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: 40.90 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 597 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeAAERAEAEKQRQKELEMQLAEEQKRLMEM-AEEERLEYQQQKLAA 675
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAA-LEALKAERQKLLARLEKELAELAAELAELqQEAEELEALIARLEA 234
|
90 100
....*....|....*....|...
gi 1907069567 676 EEKARQEAEERRKQEEEAAKLAL 698
Cdd:COG4942 235 EAAAAAERTPAAGFAALKGKLPW 257
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
597-708 |
2.73e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 597 KKRRLQLQAAR-ERARQQQEELRRKLQEIQRK-KQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKla 674
Cdd:PRK00409 528 LERELEQKAEEaEALLKEAEKLKEELEEKKEKlQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVK-- 605
|
90 100 110
....*....|....*....|....*....|....
gi 1907069567 675 aeekaRQEAEERRKQEEEAAKLALEEATKLAQEQ 708
Cdd:PRK00409 606 -----AHELIEARKRLNKANEKKEKKKKKQKEKQ 634
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
509-733 |
2.89e-03 |
|
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: 40.52 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 509 PSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQrleee 588
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 589 rqqqeeaekkrRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMqlAEEQKRLMEmAEEERLEY 668
Cdd:COG4942 89 -----------EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRR--LQYLKYLAP-ARREQAEE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907069567 669 QQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 733
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
640-714 |
3.07e-03 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 39.00 E-value: 3.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907069567 640 KQRQKELEMQLAEEQKRLMEM---AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 714
Cdd:COG0711 44 ERAKEEAEAALAEYEEKLAEAraeAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVA 121
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
604-711 |
3.81e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 40.71 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 604 QAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQ--KELEMQLAEEQKRLmemaeEERLEYQQQKlaAEEKARQ 681
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELValEGLAAELEEKQQEL-----EAQLEQLQEK--AAETSQE 213
|
90 100 110
....*....|....*....|....*....|...
gi 1907069567 682 EAEERRKQEEEAAK-LALEEAT--KLAQEQIRQ 711
Cdd:PRK11448 214 RKQKRKEITDQAAKrLELSEEEtrILIDQQLRK 246
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
463-719 |
4.22e-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: 40.72 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 463 HSAAGQLSLELDALESQVAIDGRLSSIQATDVASDMECE--EERSHEDPSKALQDKKQQEKasrDRIRIEKAEMRWLKVE 540
Cdd:TIGR00618 416 TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEklEKIHLQESAQSLKEREQQLQ---TKEQIHLQETRKKAVV 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 541 -QRRREQEELTWLHKEQLekaekMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRR 619
Cdd:TIGR00618 493 lARLLELQEEPCPLCGSC-----IHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQE 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 620 KLQEIQRKKQQEAAERAEAEKQRQKELEMQ-LAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEA-AKLA 697
Cdd:TIGR00618 568 IQQSFSILTQCDNRSKEDIPNLQNITVRLQdLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAlKLTA 647
|
250 260
....*....|....*....|...
gi 1907069567 698 LE-EATKLAQEQIRQKAALDKHL 719
Cdd:TIGR00618 648 LHaLQLTLTQERVREHALSIRVL 670
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
468-709 |
4.23e-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: 40.81 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 468 QLSLELDALESQ-VAIDGRLSSIQATDVasdmECEEERshEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVE----QR 542
Cdd:TIGR02168 751 QLSKELTELEAEiEELEERLEEAEEELA----EAEAEI--EELEAQIEQLKEELKALREALDELRAELTLLNEEaanlRE 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 543 RREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQ 622
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 623 EIQRKKQQEAAERAeaeKQRQKELEMQLAEEQKRLmemaeeeRLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEAT 702
Cdd:TIGR02168 905 ELESKRSELRRELE---ELREKLAQLELRLEGLEV-------RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRL 974
|
....*..
gi 1907069567 703 KLAQEQI 709
Cdd:TIGR02168 975 KRLENKI 981
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
608-711 |
5.17e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 38.10 E-value: 5.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 608 ERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERR 687
Cdd:pfam05672 10 EEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEERE 89
|
90 100 110
....*....|....*....|....*....|....*
gi 1907069567 688 -----------KQEEEAAKLALEEATKLAQEQIRQ 711
Cdd:pfam05672 90 qreqeeqerlqKQKEEAEAKAREEAERQRQEREKI 124
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
511-729 |
5.47e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 39.52 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 511 KALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEEltwLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQ 590
Cdd:pfam13868 35 KAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERK---RYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 591 QQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEE--RLEY 668
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREiaRLRA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907069567 669 QQQKLAAEEKARQEAEERRKQEEEAAKLALEEAtKLAQEQIRQKAALDKHLHFHQELSKEA 729
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEQERKERQKER-EEAEKKARQRQELQQAREEQIELKERR 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
515-733 |
5.60e-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: 40.43 E-value: 5.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 515 DKKQQEKASRDRIRIEKAEMrwlkVEQRRREQEELTWLHK--EQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERqqq 592
Cdd:TIGR02168 232 LRLEELREELEELQEELKEA----EEELEELTAELQELEEklEELRLEVSELEEEIEELQKELYALANEISRLEQQK--- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 593 eEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKqqeaaeraeaeKQRQKELEmQLAEEQKRLMEMAEEERLEYQQQk 672
Cdd:TIGR02168 305 -QILRERLANLERQLEELEAQLEELESKLDELAEEL-----------AELEEKLE-ELKEELESLEAELEELEAELEEL- 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907069567 673 laaeEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 733
Cdd:TIGR02168 371 ----ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
602-730 |
5.75e-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: 40.43 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 602 QLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQ------RQKELEMQLAEEQKRLMEmAEEERLEYQQQkLAA 675
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlarleaEVEQLEERIAQLSKELTE-LEAEIEELEER-LEE 772
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907069567 676 EEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAAL-DKHLHFHQELSKEAS 730
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtLLNEEAANLRERLES 828
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
597-708 |
6.39e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 6.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 597 KKRRLQLQAARERARQQQEELRRKLQEIQRKKqqeaaeraeaekqrqKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAE 676
Cdd:COG3883 139 KADKAELEAKKAELEAKLAELEALKAELEAAK---------------AELEAQQAEQEALLAQLSAEEAAAEAQLAELEA 203
|
90 100 110
....*....|....*....|....*....|..
gi 1907069567 677 EKARQEAEERRKQEEEAAKLALEEATKLAQEQ 708
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
502-728 |
7.33e-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: 7.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 502 EERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELtwLHKEQLEKAEKMKEELELEQQRRTEENRLR 581
Cdd:TIGR00618 275 QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRS--RAKLLMKRAAHVKQQSSIEEQRRLLQTLHS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 582 KQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMA 661
Cdd:TIGR00618 353 QEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQ 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 662 EEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQ-EQIRQKAALDK--HLHFHQELSKE 728
Cdd:TIGR00618 433 QELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTkEQIHLQETRKKavVLARLLELQEE 502
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
597-703 |
7.51e-03 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 39.20 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 597 KKRRLQLQAARERARQQQE--------ELRRKLQEiQRKKQqeaaeraeaekQRQKELEMQLAEEQKRLMEMAEEERLEY 668
Cdd:pfam07767 209 KKRLKEEEKLERVLEKIAEsaataearEEKRKTKA-QRNKE-----------KRRKEEEREAKEEKALKKKLAQLERLKE 276
|
90 100 110
....*....|....*....|....*....|....*
gi 1907069567 669 QQQKLAAEEKARQEAEERRKQEEEAAKLALEEATK 703
Cdd:pfam07767 277 IAKEIAEKEKEREEKAEARKREKRKKKKEEKKLRP 311
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
468-733 |
7.73e-03 |
|
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: 39.67 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 468 QLSLELDALESQVA-IDGRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQ 546
Cdd:TIGR02169 748 SLEQEIENVKSELKeLEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 547 EELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEK---KRRLQLQAARERARQQQEELRRKLQE 623
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRdleSRLGDLKKERDELEAQLRELERKIEE 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 624 IQRKKQQeaaeraeaEKQRQKELEMQLAEEQKRLMEM-AEEERLEYQQQKLAAEEKARQEaeerrKQEEEAAKLALEEAT 702
Cdd:TIGR02169 908 LEAQIEK--------KRKRLSELKAKLEALEEELSEIeDPKGEDEEIPEEELSLEDVQAE-----LQRVEEEIRALEPVN 974
|
250 260 270
....*....|....*....|....*....|..
gi 1907069567 703 KLA-QEQIRQKAALDKHLHFHQELSKEASGLQ 733
Cdd:TIGR02169 975 MLAiQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
538-713 |
8.02e-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: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 538 KVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEaekKRRLQLQAARER-------- 609
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE---REIAELEAELERldassddl 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 610 --ARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQkelemQLAEEQKRLMEMAEE-ERLEYQQQKLAAEEKARQEAEER 686
Cdd:COG4913 688 aaLEEQLEELEAELEELEEELDELKGEIGRLEKELE-----QAEEELDELQDRLEAaEDLARLELRALLEERFAAALGDA 762
|
170 180
....*....|....*....|....*..
gi 1907069567 687 RkqeEEAAKLALEEATKLAQEQIRQKA 713
Cdd:COG4913 763 V---ERELRENLEERIDALRARLNRAE 786
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
597-712 |
8.93e-03 |
|
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: 39.67 E-value: 8.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907069567 597 KKRRLQLQAARERARQQQEELRRKLQEIQRKkqqeaaeraeaEKQRQKELEMQLAEEQKRLMEMAE-EERLEYQQQKLAA 675
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRK-----------IGEIEKEIEQLEQEEEKLKERLEElEEDLSSLEQEIEN 755
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1907069567 676 EEKARQEAEER-RKQEEEAAKLALEEAT---KLAQEQIRQK 712
Cdd:TIGR02169 756 VKSELKELEARiEELEEDLHKLEEALNDleaRLSHSRIPEI 796
|
|
| |
