|
Name |
Accession |
Description |
Interval |
E-value |
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
282-792 |
1.02e-148 |
|
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: 447.48 E-value: 1.02e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 282 SSRLAQAAESQGAPQSLEAAAQKTGEPQRCINKGLICSNEKEFYTRKLHIDMTPFLKERGSELDSHEEPGGPLRGNAKDS 361
Cdd:pfam15709 3 TSPLTQTTEEQGAQQSLEAAAQKTGEPQSCINKGLICSNRKEFYTRKLHIDMTPFLKDSGEALDSHEEPGEPLGENHQDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 362 QDPELRNKTLACLSTSLAEYNQPSEADTLKSMDG-DYNVHHLHRGPLKREPAFPKKLA----SETPRKKKKRRS-KLLNQ 435
Cdd:pfam15709 83 QDPEPRSVTLSPLSASLGEHIQTPEADTVQNGDGeDYDVHHLHRGLPRHRPESPEKLTavdtSLLPRAREGKTEpRLFNQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 436 KTGVGINHG-KDLVDKAKRKKRTKTHQAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELTPKKEKLGRKMKRTHKERN 514
Cdd:pfam15709 163 ETPASISHAeRELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 515 MEMAAGLSKSDITNSKEAGGTSHQGLLRSHSAAGQ--LSLELDALESQVAIDGRLSSIQATDVASDMECEEERSHEDPSK 592
Cdd:pfam15709 243 LEVAAELSGPDVINSKETEDASERGAFSSDSVVEDpwLSSKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDPSK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 593 ALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQ 672
Cdd:pfam15709 323 ALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 673 QEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQ 752
Cdd:pfam15709 403 QEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQ 482
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 568906621 753 KLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQ 792
Cdd:pfam15709 483 KQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
549-810 |
8.74e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 75.74 E-value: 8.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 549 QLSLELDALESQVA-IDGRLSSIQATDVASDMECEEER-SHEDPSKALQDKKQQE-KASRDRIRIEKAEMRwlKVEQRRR 625
Cdd:COG1196 236 ELEAELEELEAELEeLEAELEELEAELAELEAELEELRlELEELELELEEAQAEEyELLAELARLEQDIAR--LEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 626 EQEELtwlhkEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEI 705
Cdd:COG1196 314 LEERL-----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 706 QRKKQQeaaerAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKL 785
Cdd:COG1196 389 LEALRA-----AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
250 260
....*....|....*....|....*
gi 568906621 786 AQEQIRQKAALDKHLHFHQELSKEA 810
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAE 488
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
582-798 |
2.41e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.33 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 582 EEERSHEDPSKAlQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELtwLHKEQLEKAEKMKEELELEQQRRTEENRl 661
Cdd:PTZ00121 1572 AEEDKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK--IKAEELKKAEEEKKKVEQLKKKEAEEKK- 1647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 662 rkqrLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRklQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEM 741
Cdd:PTZ00121 1648 ----KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK--AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568906621 742 --AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLA--LEEATKLAQEQIRQKAALDK 798
Cdd:PTZ00121 1722 kkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAhlKKEEEKKAEEIRKEKEAVIE 1782
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
597-814 |
4.63e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 597 KKQQEKASR-----DRIRIEKAEMRWLKVEQRRREQEELtwlhkeQLEKAEKMKEELELEQQRRTEENRLRKqrleeerq 671
Cdd:COG1196 206 ERQAEKAERyrelkEELKELEAELLLLKLRELEAELEEL------EAELEELEAELEELEAELAELEAELEE-------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 672 qqeeaekkRRLQLQAARERARQQQEELRRKLQEIQR--KKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEE----- 744
Cdd:COG1196 272 --------LRLELEELELELEEAQAEEYELLAELARleQDIARLEERRRELEERLEELEEELAELEEELEELEEEleele 343
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 745 ERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 814
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
593-814 |
1.85e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 593 ALQDKKQQEKASRDRIRIEKAEmrwlkvEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQ 672
Cdd:COG1196 231 LLKLRELEAELEELEAELEELE------AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 673 QEEaeKKRRLQLQAARERARQQQEELRRKLQEI-QRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQ 751
Cdd:COG1196 305 ARL--EERRRELEERLEELEEELAELEEELEELeEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568906621 752 QKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 814
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
549-797 |
2.53e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 549 QLSLELDALESQVAiDGRLSSIQATDVASDMECEEERSHEDPSKALQDKK-QQEKASRDRIRIEKAEMRWLKVEQRRREQ 627
Cdd:COG1196 257 ELEAELAELEAELE-ELRLELEELELELEEAQAEEYELLAELARLEQDIArLEERRRELEERLEELEEELAELEEELEEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 628 EELTwlhKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQR 707
Cdd:COG1196 336 EEEL---EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 708 KKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQ 787
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
250
....*....|
gi 568906621 788 EQIRQKAALD 797
Cdd:COG1196 493 LLLLLEAEAD 502
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
682-795 |
3.15e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 65.98 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 682 LQLQAARERARQQQEElRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKAR 761
Cdd:PRK09510 92 LQQKQAAEQERLKQLE-KERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKK 170
|
90 100 110
....*....|....*....|....*....|....
gi 568906621 762 QEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 795
Cdd:PRK09510 171 AEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAE 204
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
571-798 |
3.51e-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: 67.07 E-value: 3.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 571 QATDVASDMECEEERSHEDPSKALQDKKQQ-EKASRDRIRIEKAEMRWLKVEQRRREQEELTWlhKEQLEKAEKMKEELE 649
Cdd:pfam17380 332 QAAIYAEQERMAMERERELERIRQEERKRElERIRQEEIAMEISRMRELERLQMERQQKNERV--RQELEAARKVKILEE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 650 LEQqrRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKlQEIQRKKQQEAAERAEAEKQRQKELEM 729
Cdd:pfam17380 410 ERQ--RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQ-QQVERLRQQEEERKRKKLELEKEKRDR 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 730 QLAEEQKRLM----------EMAEEER--------LEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIR 791
Cdd:pfam17380 487 KRAEEQRRKIlekeleerkqAMIEEERkrkllekeMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERS 566
|
....*..
gi 568906621 792 QKAALDK 798
Cdd:pfam17380 567 RLEAMER 573
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
592-814 |
8.01e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 592 KALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKqrleeerq 671
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQ-------- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 672 QQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQR-QKELEMQLAEEQKRLMEMAEEERLEYQ 750
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELeELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568906621 751 QQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 814
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
582-814 |
2.13e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 64.78 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 582 EEERSHEDPSKALQDKKQQEKASRDRIR----IEKAEMRwLKVEQRRREQEELTWLHKE-----QLEKAEKMKEELELEQ 652
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKkaeeLKKAEEK-KKAEEAKKAEEDKNMALRKaeeakKAEEARIEEVMKLYEE 1603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 653 QRRTEENRLRKQRLEEERQQQ---EEAEKKRRLQLQAARERARQQQEELRRKLQEIQ------RKKQQEAAERAEAEKQR 723
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEElkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaaeeAKKAEEDKKKAEEAKKA 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 724 QKElEMQLAEEQKRlmeMAEEERLEYQQQKLAAEEKARQE----AEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKH 799
Cdd:PTZ00121 1684 EED-EKKAAEALKK---EAEEAKKAEELKKKEAEEKKKAEelkkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
|
250
....*....|....*
gi 568906621 800 LHFHQELSKEASGLQ 814
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIR 1774
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
686-810 |
8.65e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 61.75 E-value: 8.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 686 AARERARQQQEELRRKLQEIQRKKQQeaaeraeaeKQRQKELEMQLAEEQKRLMEMaEEERLEYQQQKLAAEEKARQEAE 765
Cdd:PRK09510 60 VVEQYNRQQQQQKSAKRAEEQRKKKE---------QQQAEELQQKQAAEQERLKQL-EKERLAAQEQKKQAEEAAKQAAL 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 568906621 766 ERRKQEEEAAKLA-------------LEEATKLAQEQIRQKAALDKHLHFHQELSKEA 810
Cdd:PRK09510 130 KQKQAEEAAAKAAaaakakaeaeakrAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKA 187
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
582-809 |
1.16e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 62.47 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 582 EEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLhkEQLEKAEKMKEELELEQQRRTEENRL 661
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV--EQLKKKEAEEKKKAEELKKAEEENKI 1661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 662 RKqrleeerqqqeEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraeaeKQRQKELEMQLAEEQKRlmem 741
Cdd:PTZ00121 1662 KA-----------AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE---------AKKAEELKKKEAEEKKK---- 1717
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568906621 742 AEEERLEYQQQKLAAEEKARQEAEERRKQEEeaAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKE 809
Cdd:PTZ00121 1718 AEELKKAEEENKIKAEEAKKEAEEDKKKAEE--AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
592-783 |
1.77e-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: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 592 KALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEqleKAEKMKEELELEQQRRTEENRLRKQRLEEERQ 671
Cdd:pfam17380 399 EAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEE---RAREMERVRLEEQERQQQVERLRQQEEERKRK 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 672 QQEEAEKKRRLQLQAARERA--RQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEY 749
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKilEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 568906621 750 QQQKLAAEEKARQEAEERRKQ------EEEAAKLALEEAT 783
Cdd:pfam17380 556 EQMRKATEERSRLEAMEREREmmrqivESEKARAEYEATT 595
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
678-798 |
2.74e-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: 59.86 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 678 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEyQQQKLAAE 757
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE-AKAKQAAE 131
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 568906621 758 EKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDK 798
Cdd:TIGR02794 132 AKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAK 172
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
582-794 |
3.64e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.93 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 582 EEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENR- 660
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKk 1553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 661 ---LRKQRLEEERQQQEEAEKKRRLQLQAARE--RARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMqlAEEQ 735
Cdd:PTZ00121 1554 aeeLKKAEEKKKAEEAKKAEEDKNMALRKAEEakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK--AEEE 1631
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 736 KRLMEM-----------AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKlalEEATKLAQEQIRQKA 794
Cdd:PTZ00121 1632 KKKVEQlkkkeaeekkkAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA---EEDEKKAAEALKKEA 1698
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
582-798 |
4.32e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.54 E-value: 4.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 582 EEERSHEDPSKAlQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQL----EKAEKMKEELELEQQRRTE 657
Cdd:PTZ00121 1215 EEARKAEDAKKA-EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaikaEEARKADELKKAEEKKKAD 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 658 ENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQE------IQRKKQQEAAERAEAEKQRQKELEMQL 731
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEakkaaeAAKAEAEAAADEAEAAEEKAEAAEKKK 1373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 732 AEEQKR---LMEMAEEERLEYQQQKLAAEEKarQEAEERRKQEEEAAKlaLEEATKLAQEQIRQKAALDK 798
Cdd:PTZ00121 1374 EEAKKKadaAKKKAEEKKKADEAKKKAEEDK--KKADELKKAAAAKKK--ADEAKKKAEEKKKADEAKKK 1439
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
579-798 |
1.00e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.92 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 579 MECEEERSHEDPSKALQDKKQQEKASRDRIRieKAEMRWLKVEQRRREQEEltwlhKEQLEKAEKMKEELELEQQRRTEE 658
Cdd:PTZ00121 1272 IKAEEARKADELKKAEEKKKADEAKKAEEKK--KADEAKKKAEEAKKADEA-----KKKAEEAKKKADAAKKKAEEAKKA 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 659 NRLRKQRLEEERQQQEEAEKKRRLQlQAARERARQQQEELRRKLQEIqrKKQQEAAERAEAEKQRQKELEMQLAEEQK-- 736
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEAA-EKKKEEAKKKADAAKKKAEEK--KKADEAKKKAEEDKKKADELKKAAAAKKKad 1421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568906621 737 RLMEMAEEERLEYQQQKLAAE----EKARQEAEERRKQEE-----EAAKLAlEEATKLAQEQIRQKAALDK 798
Cdd:PTZ00121 1422 EAKKKAEEKKKADEAKKKAEEakkaDEAKKKAEEAKKAEEakkkaEEAKKA-DEAKKKAEEAKKADEAKKK 1491
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
461-808 |
1.37e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 461 QAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELTPKKEKLGRKMKRTHKERNMEMAAGLSKSDITNSKEAGGTSHQGL 540
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 541 LRSHSAAGQLSLELDALESQVAIDGRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKV 620
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 621 EQRRREQEELTwlhKEQLEKAEKMKEELELEQQRRTEENRLR---KQRLEEERQQQEEAEKKRRLQLQAARERarqQQEE 697
Cdd:PTZ00121 1401 EEDKKKADELK---KAAAAKKKADEAKKKAEEKKKADEAKKKaeeAKKADEAKKKAEEAKKAEEAKKKAEEAK---KADE 1474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 698 LRRKLQEIQRK---KQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKarQEAEERRKQEE-- 772
Cdd:PTZ00121 1475 AKKKAEEAKKAdeaKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA--KKAEEKKKADElk 1552
|
330 340 350
....*....|....*....|....*....|....*.
gi 568906621 773 EAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSK 808
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
592-789 |
1.64e-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: 55.06 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 592 KALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHK-EQLEKAEKMKEELELEQQRRTEENRLRKQRLEEER 670
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 671 QQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRK--KQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEerLE 748
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAE--IE 862
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568906621 749 YQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQ 789
Cdd:TIGR02168 863 ELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
550-828 |
1.94e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 550 LSLELDALESQ-VAIDGRLSSIQA--TDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQR--R 624
Cdd:TIGR02169 228 LLKEKEALERQkEAIERQLASLEEelEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAslE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 625 REQEELtwlhKEQLEKAEKmkeeleleQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQE 704
Cdd:TIGR02169 308 RSIAEK----ERELEDAEE--------RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 705 IQRKKQqeaaERAEAEKQRQKELEM------QLAEEQKRLMEMAE---------EERLEYQQQKLAAEEKARQEAEERRK 769
Cdd:TIGR02169 376 VDKEFA----ETRDELKDYREKLEKlkreinELKRELDRLQEELQrlseeladlNAAIAGIEAKINELEEEKEDKALEIK 451
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 568906621 770 QEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQWTQNISRPWVYSYF 828
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
685-810 |
2.00e-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: 54.08 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 685 QAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRlmemAEEERLEYQQQKLAAEEKARQEA 764
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAA----AEKAAKQAEQAAKQAEEKQKQAE 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568906621 765 EERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEA 810
Cdd:TIGR02794 123 EAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKA 168
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
592-792 |
5.72e-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: 53.20 E-value: 5.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 592 KALQDKKQQEKASR---DRIRIEKAEmRWLKVEQRRR--------------------EQEELTWLHKEQLEKAEKMKEEL 648
Cdd:pfam17380 282 KAVSERQQQEKFEKmeqERLRQEKEE-KAREVERRRKleeaekarqaemdrqaaiyaEQERMAMERERELERIRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 649 ELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRL--QLQAAReRARQQQEELRRKLQEIQRKKQQeaaERAEAEKQRQKE 726
Cdd:pfam17380 361 ELERIRQEEIAMEISRMRELERLQMERQQKNERVrqELEAAR-KVKILEEERQRKIQQQKVEMEQ---IRAEQEEARQRE 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568906621 727 LEmQLAEEQKRLMEMAEEERLEYQQQKlaaeEKARQEAEERRKQEEEAAKlaLEEATKLAQEQIRQ 792
Cdd:pfam17380 437 VR-RLEEERAREMERVRLEEQERQQQV----ERLRQQEEERKRKKLELEK--EKRDRKRAEEQRRK 495
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
685-795 |
5.82e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 52.95 E-value: 5.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 685 QAARERARQQQEELRRklQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLmEMAEEERLEyQQQKLAAEEKARQEA 764
Cdd:COG2268 241 EAEAELAKKKAEERRE--AETARAEAEAAYEIAEANAEREVQRQLEIAEREREI-ELQEKEAER-EEAELEADVRKPAEA 316
|
90 100 110
....*....|....*....|....*....|..
gi 568906621 765 EERRKQEEEAAKLALEEATKLAQ-EQIRQKAA 795
Cdd:COG2268 317 EKQAAEAEAEAEAEAIRAKGLAEaEGKRALAE 348
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
655-810 |
1.36e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 655 RTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQ-EAAERAEAEKQRQKELEMQLAE 733
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568906621 734 EQKRLMEMaeEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEA 810
Cdd:COG4717 144 LPERLEEL--EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
588-798 |
3.73e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.26 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 588 EDPSKAL--QDKKQQEKASRDRiRIEKAEMRW---LKVEQRRREQEEltwlhkEQLEKAEKMKEELELEQQRRTEEnrlr 662
Cdd:COG2268 180 EDENNYLdaLGRRKIAEIIRDA-RIAEAEAEReteIAIAQANREAEE------AELEQEREIETARIAEAEAELAK---- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 663 kqrleeerqqqeeaeKKRRLQLQAARERARQQQE-ELRR--KLQEIQRKKQQEaaeraeaekQRQKELEMQLAEEQKRLM 739
Cdd:COG2268 249 ---------------KKAEERREAETARAEAEAAyEIAEanAEREVQRQLEIA---------EREREIELQEKEAEREEA 304
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568906621 740 EMAEEERLEYQQQKLAAEEKARQEAE-ERRKQEEEA-AKLALEEATKLAQEQIRQKAALDK 798
Cdd:COG2268 305 ELEADVRKPAEAEKQAAEAEAEAEAEaIRAKGLAEAeGKRALAEAWNKLGDAAILLMLIEK 365
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
538-788 |
3.87e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 3.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 538 QGLLRSHSAAGQLSLELDALESQVAidgRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRdRIRIEKAEMRW 617
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELA---ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA-LLEAEAELAEA 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 618 LKVEQRRREQEEltwlhkeQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEE 697
Cdd:COG1196 378 EEELEELAEELL-------EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 698 LRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKL 777
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
|
250
....*....|.
gi 568906621 778 ALEEATKLAQE 788
Cdd:COG1196 531 GVEAAYEAALE 541
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
592-796 |
9.00e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 592 KALQDKKQQ-EKASRDRIRIEKAEMRWL--KVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEE 668
Cdd:COG4717 49 ERLEKEADElFKPQGRKPELNLKELKELeeELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 669 ERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaerAEAEKQRQKELEMQLAEEQKRLMEMAEEERLE 748
Cdd:COG4717 129 PLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE-----LAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 568906621 749 YQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAAL 796
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
678-788 |
9.65e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.01 E-value: 9.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 678 KKRRLQLQAARERARQQQEELRRKLQEIQRK------KQQEAAERAEAEKQRQKELEMQLAEEQKRL------------- 738
Cdd:PRK12704 78 RERRNELQKLEKRLLQKEENLDRKLELLEKReeelekKEKELEQKQQELEKKEEELEELIEEQLQELerisgltaeeake 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568906621 739 --MEMAEEErleyqqqklaaeekARQEAEERRKQEEEAAKlalEEATKLAQE 788
Cdd:PRK12704 158 ilLEKVEEE--------------ARHEAAVLIKEIEEEAK---EEADKKAKE 192
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
592-802 |
1.01e-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: 48.61 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 592 KALQDKKQQEKASRDRIR--IEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEE--NRLRKQRLE 667
Cdd:COG4942 37 AELEKELAALKKEEKALLkqLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElaELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 668 EERQQQE-------EAEKKRRLQLQAARERARQQQ-EELRRKLQEIQRKKQQeaaerAEAEKQRQKELEMQLAEEQKRLm 739
Cdd:COG4942 117 GRQPPLAlllspedFLDAVRRLQYLKYLAPARREQaEELRADLAELAALRAE-----LEAERAELEALLAELEEERAAL- 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568906621 740 emaeeERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHF 802
Cdd:COG4942 191 -----EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
678-804 |
1.29e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 678 KKRRLQLQAARERARQQQE-ELRRKLQEIQRKKQQEaaeraeaeKQRQKELEMQLAEEQKRlmemaeEERLEYQQQKLAA 756
Cdd:PRK12704 56 KEALLEAKEEIHKLRNEFEkELRERRNELQKLEKRL--------LQKEENLDRKLELLEKR------EEELEKKEKELEQ 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 568906621 757 E----EKARQEAEERRKQE----EEAAKLALEEATKLAQEQIRQKAALDKHLHFHQ 804
Cdd:PRK12704 122 KqqelEKKEEELEELIEEQlqelERISGLTAEEAKEILLEKVEEEARHEAAVLIKE 177
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
582-779 |
1.39e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 582 EEERSHEDPSKALQDKKQQEKASRDRIRIEKAEmrwLKVEQRRREQEELTWLHKEQLEKAEkmkeeleleQQRRTEENRL 661
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEE---LREELEKLEKLLQLLPLYQELEALE---------AELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 662 RKQRLEEerqqqeeaekKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEm 741
Cdd:COG4717 149 EELEERL----------EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE- 217
|
170 180 190
....*....|....*....|....*....|....*...
gi 568906621 742 aEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLAL 779
Cdd:COG4717 218 -AQEELEELEEELEQLENELEAAALEERLKEARLLLLI 254
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
595-795 |
1.53e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 48.33 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 595 QDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQE 674
Cdd:pfam02029 143 NKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVT 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 675 EAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRlmemAEEERleyqqqkl 754
Cdd:pfam02029 223 TKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKK----REERR-------- 290
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 568906621 755 aaeeKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 795
Cdd:pfam02029 291 ----KLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERRRA 327
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
549-786 |
1.76e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 549 QLSLELDALESQVAI-DGRLSSIQATDVASDMECEEERSHEDPSKA----LQDKKQQEKASRDRIRIEKAEMRWLKVEQR 623
Cdd:TIGR02168 292 ALANEISRLEQQKQIlRERLANLERQLEELEAQLEELESKLDELAEelaeLEEKLEELKEELESLEAELEELEAELEELE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 624 RREQEEltwlhKEQLEKAEKMKEELEleQQRRTEENRLRkqrleeerqqqeeAEKKRRLQLQAARERARQQQEELRRKLQ 703
Cdd:TIGR02168 372 SRLEEL-----EEQLETLRSKVAQLE--LQIASLNNEIE-------------RLEARLERLEDRRERLQQEIEELLKKLE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 704 EIQRKKQQEA----AERAEAEKQRQKELEMQLAEEQKRLMEMAEEER-LEYQQQKLAAEEKARQEAEERRKQEEEAAKLA 778
Cdd:TIGR02168 432 EAELKELQAEleelEEELEELQEELERLEEALEELREELEEAEQALDaAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
....*...
gi 568906621 779 LEEATKLA 786
Cdd:TIGR02168 512 LKNQSGLS 519
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
580-765 |
2.18e-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: 48.20 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 580 ECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKaekmkeeLELEQQRRTEEN 659
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEK-------EKRDRKRAEEQR 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 660 R-LRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraEAEKQRQKELEMQLAEEQKRL 738
Cdd:pfam17380 494 RkILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQ------EMEERRRIQEQMRKATEERSR 567
|
170 180
....*....|....*....|....*..
gi 568906621 739 MEMAEEERLEYQQqkLAAEEKARQEAE 765
Cdd:pfam17380 568 LEAMEREREMMRQ--IVESEKARAEYE 592
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
597-814 |
2.62e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 597 KKQQEKASRDR-IRIEKAEMRW----LKVEQRRREQEELtwlhKEQLEKAEKMKEELELEQQRRTEE-NRLRKQrleeer 670
Cdd:TIGR02168 206 ERQAEKAERYKeLKAELRELELallvLRLEELREELEEL----QEELKEAEEELEELTAELQELEEKlEELRLE------ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 671 qqqEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraeaEKQRQKELEMQLAEEQKRLMEMAEE-ERLEY 749
Cdd:TIGR02168 276 ---VSELEEEIEELQKELYALANEISRLEQQKQILRERLAN--------LERQLEELEAQLEELESKLDELAEElAELEE 344
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568906621 750 QQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQ-------IRQKAALDKHLhfhQELSKEASGLQ 814
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLrskvaqlELQIASLNNEI---ERLEARLERLE 413
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
678-798 |
2.66e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 47.78 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 678 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAE-----EERLEYQQQ 752
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEkldnlENQLEEREK 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 568906621 753 KLAAEEKARQEAEERRKQE-EEAAKLALEEATKLAQEQIRQKAALDK 798
Cdd:PRK12705 113 ALSARELELEELEKQLDNElYRVAGLTPEQARKLLLKLLDAELEEEK 159
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
582-791 |
3.10e-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: 47.76 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 582 EEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEEltwlHKEQLE-KAEKMKEELELEQQRRTEENR 660
Cdd:TIGR02169 204 RREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE----ELEKLTeEISELEKRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 661 lrkqRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeAAERAEAEKQRQKELEMQLAEEQKRLME 740
Cdd:TIGR02169 280 ----KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK-LEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 568906621 741 MAEE-----ERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIR 791
Cdd:TIGR02169 355 LTEEyaelkEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
584-795 |
3.10e-05 |
|
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: 46.84 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 584 ERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRK 663
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 664 qrleeerqqqeeaekkRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEM------QLAEEQKR 737
Cdd:pfam13868 188 ----------------RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELqqareeQIELKERR 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 568906621 738 LMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLAlEEATKLAQEQIRQKAA 795
Cdd:pfam13868 252 LAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHR-RELEKQIEEREEQRAA 308
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
652-800 |
3.89e-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: 46.92 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 652 QQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQL 731
Cdd:pfam05262 204 KERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREI 283
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568906621 732 AEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLaQEQIRQKAALDKHL 800
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 ... |
621-798 |
4.45e-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: 46.38 E-value: 4.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 621 EQRRREQEELtwlhkEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRR 700
Cdd:TIGR02794 61 PAAKKEQERQ-----KKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 701 KLQEIQRKKQQEAaeraeaEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEaEERRKQEEEAAKLALE 780
Cdd:TIGR02794 136 AEAEAERKAKEEA------AKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAE-EAKAKAEAAKAKAAAE 208
|
170
....*....|....*...
gi 568906621 781 EATKLAQEQIRQKAALDK 798
Cdd:TIGR02794 209 AAAKAEAEAAAAAAAEAE 226
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
683-795 |
4.79e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 683 QLQAARERARQQQEELRRKLQEIQRKKQQEaaeraeaeKQRQKELEMQLAEEQKRLMEMAEEERlEYQQQKlAAEEKARQ 762
Cdd:COG3883 137 ELKADKAELEAKKAELEAKLAELEALKAEL--------EAAKAELEAQQAEQEALLAQLSAEEA-AAEAQL-AELEAELA 206
|
90 100 110
....*....|....*....|....*....|...
gi 568906621 763 EAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 795
Cdd:COG3883 207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
683-807 |
5.71e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.97 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 683 QLQAARERAR----------QQQEELRRKLQEIQRKKQ----------QEAAERAEAEKQRQK----ELEM-QL-AEEQK 736
Cdd:PRK10929 124 QAQQEQDRAReisdslsqlpQQQTEARRQLNEIERRLQtlgtpntplaQAQLTALQAESAALKalvdELELaQLsANNRQ 203
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568906621 737 RLMEMAEE------ERLEYQQQKLaaeekaRQEAEERRKQEeeaAKLALEEATKLAQEQIRQKAALDKHLHFHQELS 807
Cdd:PRK10929 204 ELARLRSElakkrsQQLDAYLQAL------RNQLNSQRQRE---AERALESTELLAEQSGDLPKSIVAQFKINRELS 271
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
598-809 |
6.37e-05 |
|
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: 46.07 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 598 KQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRrtEENRLRKQRLEEERQQQEEAE 677
Cdd:pfam13868 26 AQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQI--EEREQKRQEEYEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 678 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAE-----EQKRLMEMAEEERLEYQQQ 752
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEylkekAEREEEREAEREEIEEEKE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 568906621 753 KLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKE 809
Cdd:pfam13868 184 REIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQA 240
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
621-798 |
7.45e-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: 46.50 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 621 EQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQL--QAARERARQQQEEL 698
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLdyLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 699 RRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLA 778
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180
....*....|....*....|
gi 568906621 779 LEEATKLAQEQIRQKAALDK 798
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELK 345
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
619-795 |
1.31e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 619 KVEQRRREQEEltwlhKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEEL 698
Cdd:PRK09510 71 QKSAKRAEEQR-----KKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 699 RRKlQEIQRKKQQEAAERAEAEKQRQKElemqlAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLA 778
Cdd:PRK09510 146 KAK-AEAEAKRAAAAAKKAAAEAKKKAE-----AEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKA 219
|
170
....*....|....*..
gi 568906621 779 LEEATKLAQEQIRQKAA 795
Cdd:PRK09510 220 AAEAKAAAAKAAAEAKA 236
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
689-773 |
1.40e-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: 43.11 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 689 ERARQQQEELRRKLQEiQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEY-QQQKLAAEEKARQEAEER 767
Cdd:pfam05672 39 EEERLRKEELRRRAEE-ERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERlQKQKEEAEAKAREEAERQ 117
|
....*.
gi 568906621 768 RKQEEE 773
Cdd:pfam05672 118 RQEREK 123
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
678-809 |
1.52e-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: 45.23 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 678 KKRRLQLQAARerarQQQEELRRKL-----------QEIQRKKQ-----QEAAERAEAEKQRQKE--------------- 726
Cdd:pfam09726 405 KKLKAELQASR----QTEQELRSQIssltslerslkSELGQLRQendllQTKLHNAVSAKQKDKQtvqqlekrlkaeqea 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 727 ---LEMQLAEEQKRLMEmaEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFH 803
Cdd:pfam09726 481 rasAEKQLAEEKKRKKE--EEATAARAVALAAASRGECTESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQELRKY 558
|
....*.
gi 568906621 804 QELSKE 809
Cdd:pfam09726 559 KESEKD 564
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
611-781 |
1.64e-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: 44.52 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 611 EKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQeeaeKKRRLQLQAARER 690
Cdd:pfam13868 166 EREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE----KKARQRQELQQAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 691 ARQQQEELRRKLQEIQR---------KKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKAR 761
Cdd:pfam13868 242 EEQIELKERRLAEEAEReeeefermlRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLR 321
|
170 180
....*....|....*....|
gi 568906621 762 QEAEERRKQEEEAAKLALEE 781
Cdd:pfam13868 322 EEEAERRERIEEERQKKLKE 341
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
601-814 |
2.02e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 601 EKASRDRIRIEKAEMRWLK-----VEQRRREQEELTWL--HKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQ 673
Cdd:COG4913 220 EPDTFEAADALVEHFDDLEraheaLEDAREQIELLEPIreLAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 674 EEAEKKRrlqLQAARERARQQQEELRRKLQEIQRKKQQEAAeraeaekQRQKELEMQLAEEQKRLMEmAEEERLEYQQQK 753
Cdd:COG4913 300 LRAELAR---LEAELERLEARLDALREELDELEAQIRGNGG-------DRLEQLEREIERLERELEE-RERRRARLEALL 368
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568906621 754 LAAEEKARQEAEE--RRKQEEEAAKLALEEATKLAQEQIRQ-KAALDKHLHFHQELSKEASGLQ 814
Cdd:COG4913 369 AALGLPLPASAEEfaALRAEAAALLEALEEELEALEEALAEaEAALRDLRRELRELEAEIASLE 432
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
597-821 |
2.27e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.83 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 597 KKQQEKASRDRIRIEKAEMRWLK-----VEQRRREQEELTwLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQ 671
Cdd:pfam12128 311 SAADAAVAKDRSELEALEDQHGAfldadIETAAADQEQLP-SWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNN 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 672 QQEEAEKKRRlqlQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLME-MAEEERLEYQ 750
Cdd:pfam12128 390 RDIAGIKDKL---AKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQaTATPELLLQL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 751 QQKLAAEEKARQEAEERRKQ------EEEAAKLALEEAT-KLAQEQIR---QKAALDKHLH--------FHQELSKEASG 812
Cdd:pfam12128 467 ENFDERIERAREEQEAANAEverlqsELRQARKRRDQASeALRQASRRleeRQSALDELELqlfpqagtLLHFLRKEAPD 546
|
....*....
gi 568906621 813 lqWTQNISR 821
Cdd:pfam12128 547 --WEQSIGK 553
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
537-818 |
2.50e-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: 45.05 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 537 HQGLLRSHSAAGQLSLELDALESQV-AIDGRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQekasrdRIRIEKAEM 615
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELqELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ------QKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 616 RWLKVEQRRREqeeltwlhkEQLEKAEkmkeELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQ 695
Cdd:TIGR02168 312 ANLERQLEELE---------AQLEELE----SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 696 EELRRKLQEIQRKKQQEAAERAeaekqRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAA 775
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNN-----EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ 453
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 568906621 776 K--LALEEATKLAQEQIRQK-AALDKHLHFHQELSKEASGLQWTQN 818
Cdd:TIGR02168 454 EelERLEEALEELREELEEAeQALDAAERELAQLQARLDSLERLQE 499
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
599-809 |
2.57e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.73 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 599 QQEKASRDRIRIEKAEmrwlKVEQRRREQEeltwlhKEQLEKaekmkeelelEQQRRTEENRLRKQRLEEERQQQEEAEK 678
Cdd:pfam17380 279 QHQKAVSERQQQEKFE----KMEQERLRQE------KEEKAR----------EVERRRKLEEAEKARQAEMDRQAAIYAE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 679 KRRLQLQAARERARQQQEELRRKLQEI----------------------QRKKQQEAAERAEAEKQRQKELEMQ-LAEEQ 735
Cdd:pfam17380 339 QERMAMERERELERIRQEERKRELERIrqeeiameisrmrelerlqmerQQKNERVRQELEAARKVKILEEERQrKIQQQ 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568906621 736 KRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKE 809
Cdd:pfam17380 419 KVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ 492
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
461-795 |
2.61e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 461 QAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELtpkKEKLGRKMKRTHKERNMEMAAGLSKSDITNSKEAGGTshQGL 540
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAEL---LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL--RGL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 541 LRSHSAAGQLSLELDALEsQVAIDGRLSSIQATDVASDMECEEERSHEDPSKA----LQDKKQQEKASRDRIRIEKAEMR 616
Cdd:COG1196 523 AGAVAVLIGVEAAYEAAL-EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflpLDKIRARAALAAALARGAIGAAV 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 617 WLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLR-KQRLEEERQQQEEAEKKRRLQLQAARERARQQQ 695
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLReVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 696 EELRRKLQEIQRKKQQeaaeraeaeKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAA 775
Cdd:COG1196 682 EELAERLAEEELELEE---------ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
330 340
....*....|....*....|
gi 568906621 776 KLALEEATKLAQEQIRQKAA 795
Cdd:COG1196 753 LEELPEPPDLEELERELERL 772
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
567-809 |
3.93e-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: 44.19 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 567 LSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKV-EQRRREQEELTWLHKEQLEKAEKMK 645
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERrKVDDEEKLKESEKEKKKAEKELKKE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 646 EELELEQQRRTEENRLRKQRLEEERQQqeeaekkrrlqlqaarerARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQK 725
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAEEEEEEE------------------LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 726 ELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEaAKLALEEATKLAQEQIRQKAALDKHLHFHQE 805
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ-GKLTEEKEELEKQELKLLKDELELKKSEDLL 474
|
....
gi 568906621 806 LSKE 809
Cdd:pfam02463 475 KETQ 478
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
595-786 |
4.62e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.80 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 595 QDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEEltWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQE 674
Cdd:TIGR00618 208 LCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH--AYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQER 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 675 EAEKKRRLQL---QAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQkrLMEMAEEERLEYQQ 751
Cdd:TIGR00618 286 INRARKAAPLaahIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT--LHSQEIHIRDAHEV 363
|
170 180 190
....*....|....*....|....*....|....*
gi 568906621 752 QKLAAEEKARQEAEERRKQEEEAAKLALEEATKLA 786
Cdd:TIGR00618 364 ATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSL 398
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
672-776 |
4.95e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 4.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 672 QQEEAEKKRRLQLQAARERARQQQEELRRKLQEiQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEM-AEEERLEYQ 750
Cdd:PRK11637 170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYE-QQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELrANESRLRDS 248
|
90 100 110
....*....|....*....|....*....|.
gi 568906621 751 QQKLAAEEKARQEAEER-----RKQEEEAAK 776
Cdd:PRK11637 249 IARAEREAKARAEREAReaarvRDKQKQAKR 279
|
|
| DDRGK |
pfam09756 |
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ... |
700-774 |
5.10e-04 |
|
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: 41.95 E-value: 5.10e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568906621 700 RKLQEIQRKKQQEAAEraeaeKQRQKELEMQLAEEQKRLMEMAEEERLEYQ-QQKLAAEEKARQEA---EERRKQEEEA 774
Cdd:pfam09756 1 KKLGAKKRAKLELKEA-----KRQQREAEEEEREEREKLEEKREEEYKEREeREEEAEKEKEEEERkqeEEQERKEQEE 74
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
721-795 |
5.81e-04 |
|
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: 40.50 E-value: 5.81e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568906621 721 KQRQKELEMQLAEEQKRLMEM---AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 795
Cdd:cd06503 43 EKAKEEAEELLAEYEEKLAEAraeAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVA 120
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
580-810 |
6.71e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 580 ECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEEN 659
Cdd:pfam02463 195 LKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKEN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 660 RLRKQRLEEERQQQEEAEKKRRlQLQAARERARQQQEELRRKLQEIQR---------KKQQEAAERAEAEKQRQ--KELE 728
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEE-ELKSELLKLERRKVDDEEKLKESEKekkkaekelKKEKEEIEELEKELKELeiKREA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 729 MQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRkqEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSK 808
Cdd:pfam02463 354 EEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK--EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEI 431
|
..
gi 568906621 809 EA 810
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 ... |
549-783 |
7.96e-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: 7.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 549 QLSLELDALESQVaidgrLSSIQATDVASDMECEEERSHEDPSKaLQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQE 628
Cdd:pfam02463 268 AQVLKENKEEEKE-----KKLQEEELKLLAKEEEELKSELLKLE-RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 629 ELTWLHKEQLEKAEKMKEEleLEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAAR----ERARQQQEELRRKLQE 704
Cdd:pfam02463 342 KELKELEIKREAEEEEEEE--LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELkseeEKEAQLLLELARQLED 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 705 IQRKKQQEAAERAEAEKQRQKELEMQLAEEQ-KRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEAT 783
Cdd:pfam02463 420 LLKEEKKEELEILEEEEESIELKQGKLTEEKeELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERS 499
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
696-798 |
9.37e-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: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 696 EELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMaeEERLEYQQQKLAAEEKARQEAEERRKQEEEaa 775
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEAL--KARWEAEKELIEEIQELKEELEQRYGKIPE-- 489
|
90 100
....*....|....*....|...
gi 568906621 776 klaLEEATKLAQEQIRQKAALDK 798
Cdd:COG0542 490 ---LEKELAELEEELAELAPLLR 509
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
460-794 |
1.11e-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: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 460 HQAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELTPKKEKLGRKMKRTHKERNMEMAAGLSKSDITNSKEAGGTSHQG 539
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 540 LLRSHSAAGQLSLELDALESQVAIDGRLSSIQATDVASDMECEEE----------RSHEDPSKALQDKKQQEKASRDRIR 609
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaaalqnivvEDDEVAAAAIEYLKAAKAGRATFLP 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 610 IEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARE 689
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 690 RARQQQEELRRKLQEIQRKKQQEAAE--RAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEER 767
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELaeRLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
330 340
....*....|....*....|....*..
gi 568906621 768 RKQEEEAAKLALEEATKLAQEQIRQKA 794
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEEL 765
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
592-810 |
1.15e-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: 42.21 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 592 KALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEEltwLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQ 671
Cdd:pfam13868 35 KAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERK---RYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 672 QQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEE--RLEY 749
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREiaRLRA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568906621 750 QQQKLAAEEKARQEAEERRKQEEEAAKLALEEAtKLAQEQIRQKAALDKHLHFHQELSKEA 810
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEQERKERQKER-EEAEKKARQRQELQQAREEQIELKERR 251
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
544-800 |
1.25e-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: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 544 HSAAGQLSLELDALESQVAIDGRLSSIQATDVASDMECE--EERSHEDPSKALQDKKQQEKasrDRIRIEKAEMRWLKVE 621
Cdd:TIGR00618 416 TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEklEKIHLQESAQSLKEREQQLQ---TKEQIHLQETRKKAVV 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 622 -QRRREQEELTWLHKEQLekaekMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRR 700
Cdd:TIGR00618 493 lARLLELQEEPCPLCGSC-----IHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQE 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 701 KLQEIQRKKQQEAAERAEAEKQRQKELEMQ-LAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEA-AKLA 778
Cdd:TIGR00618 568 IQQSFSILTQCDNRSKEDIPNLQNITVRLQdLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAlKLTA 647
|
250 260
....*....|....*....|...
gi 568906621 779 LE-EATKLAQEQIRQKAALDKHL 800
Cdd:TIGR00618 648 LHaLQLTLTQERVREHALSIRVL 670
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
721-795 |
1.39e-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: 40.16 E-value: 1.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568906621 721 KQRQKELEMQLAEEQKRLMEM---AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 795
Cdd:COG0711 44 ERAKEEAEAALAEYEEKLAEAraeAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVA 121
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
593-772 |
1.45e-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: 41.83 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 593 ALQDKKQQEKASRDRIRIEKAEMRWLKvEQRRREQEEltwlhkeqlekaekmkeelelEQQRRTEENRLRKQRLEEERQq 672
Cdd:pfam13868 191 AQQEKAQDEKAERDELRAKLYQEEQER-KERQKEREE---------------------AEKKARQRQELQQAREEQIEL- 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 673 qeeaekkRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAE-EQKRLMEMAEEERLEYQQ 751
Cdd:pfam13868 248 -------KERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEErEEQRAAEREEELEEGERL 320
|
170 180
....*....|....*....|.
gi 568906621 752 QKLAAEEKARQEAEERRKQEE 772
Cdd:pfam13868 321 REEEAERRERIEEERQKKLKE 341
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
590-814 |
1.54e-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: 41.67 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 590 PSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQrleee 669
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 670 rqqqeeaekkrRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMqlAEEQKRLMEmAEEERLEY 749
Cdd:COG4942 89 -----------EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRR--LQYLKYLAP-ARREQAEE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568906621 750 QQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 814
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
678-779 |
1.55e-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: 41.67 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 678 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeAAERAEAEKQRQKELEMQLAEEQKRLMEM-AEEERLEYQQQKLAA 756
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAA-LEALKAERQKLLARLEKELAELAAELAELqQEAEELEALIARLEA 234
|
90 100
....*....|....*....|...
gi 568906621 757 EEKARQEAEERRKQEEEAAKLAL 779
Cdd:COG4942 235 EAAAAAERTPAAGFAALKGKLPW 257
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
689-792 |
2.05e-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: 39.64 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 689 ERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERR 768
Cdd:pfam05672 10 EEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEERE 89
|
90 100 110
....*....|....*....|....*....|....*
gi 568906621 769 -----------KQEEEAAKLALEEATKLAQEQIRQ 792
Cdd:pfam05672 90 qreqeeqerlqKQKEEAEAKAREEAERQRQEREKI 124
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
582-814 |
2.52e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 582 EEERSHEdpsKALQ-DKKQQEKASRDRIRIEKAEMrwlkVEQRRREQEELTWLHK--EQLEKAEKMKEELELEQQRRTEE 658
Cdd:TIGR02168 220 AELRELE---LALLvLRLEELREELEELQEELKEA----EEELEELTAELQELEEklEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 659 NRLRKQRLEEERqqqeEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKqqeaaeraeaeKQRQKELEmQLAEEQKRL 738
Cdd:TIGR02168 293 LANEISRLEQQK----QILRERLANLERQLEELEAQLEELESKLDELAEEL-----------AELEEKLE-ELKEELESL 356
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568906621 739 MEMAEEERLEYQQQklaaeEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 814
Cdd:TIGR02168 357 EAELEELEAELEEL-----ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
549-790 |
2.65e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 549 QLSLELDALESQ-VAIDGRLSSIQATDVasdmECEEERshEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVE----QR 623
Cdd:TIGR02168 751 QLSKELTELEAEiEELEERLEEAEEELA----EAEAEI--EELEAQIEQLKEELKALREALDELRAELTLLNEEaanlRE 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 624 RREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQ 703
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 704 EIQRKKQQEAAERAeaeKQRQKELEMQLAEEQKRLmemaeeeRLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEAT 783
Cdd:TIGR02168 905 ELESKRSELRRELE---ELREKLAQLELRLEGLEV-------RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRL 974
|
....*..
gi 568906621 784 KLAQEQI 790
Cdd:TIGR02168 975 KRLENKI 981
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
678-789 |
2.87e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.35 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 678 KKRRLQLQAAR-ERARQQQEELRRKLQEIQRK-KQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKla 755
Cdd:PRK00409 528 LERELEQKAEEaEALLKEAEKLKEELEEKKEKlQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVK-- 605
|
90 100 110
....*....|....*....|....*....|....
gi 568906621 756 aeekaRQEAEERRKQEEEAAKLALEEATKLAQEQ 789
Cdd:PRK00409 606 -----AHELIEARKRLNKANEKKEKKKKKQKEKQ 634
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
683-811 |
3.25e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 683 QLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQ------RQKELEMQLAEEQKRLMEmAEEERLEYQQQkLAA 756
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlarleaEVEQLEERIAQLSKELTE-LEAEIEELEER-LEE 772
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 568906621 757 EEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAAL-DKHLHFHQELSKEAS 811
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtLLNEEAANLRERLES 828
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
679-777 |
3.29e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 38.36 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 679 KRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEyqQQKLAAEE 758
Cdd:pfam20492 13 ERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLE--AELAEAQE 90
|
90
....*....|....*....
gi 568906621 759 KARQEAEERRKQEEEAAKL 777
Cdd:pfam20492 91 EIARLEEEVERKEEEARRL 109
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
685-792 |
3.81e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 685 QAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQ--KELEMQLAEEQKRLmemaeEERLEYQQQKlaAEEKARQ 762
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELValEGLAAELEEKQQEL-----EAQLEQLQEK--AAETSQE 213
|
90 100 110
....*....|....*....|....*....|...
gi 568906621 763 EAEERRKQEEEAAK-LALEEAT--KLAQEQIRQ 792
Cdd:PRK11448 214 RKQKRKEITDQAAKrLELSEEEtrILIDQQLRK 246
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
583-809 |
3.93e-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: 41.11 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 583 EERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELtwLHKEQLEKAEKMKEELELEQQRRTEENRLR 662
Cdd:TIGR00618 275 QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRS--RAKLLMKRAAHVKQQSSIEEQRRLLQTLHS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 663 KQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMA 742
Cdd:TIGR00618 353 QEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQ 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 743 EEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQ-EQIRQKAALDK--HLHFHQELSKE 809
Cdd:TIGR00618 433 QELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTkEQIHLQETRKKavVLARLLELQEE 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
549-814 |
4.48e-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: 40.82 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 549 QLSLELDALESQVA-IDGRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQ 627
Cdd:TIGR02169 748 SLEQEIENVKSELKeLEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 628 EELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEK---KRRLQLQAARERARQQQEELRRKLQE 704
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRdleSRLGDLKKERDELEAQLRELERKIEE 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 705 IQRKKQQeaaeraeaEKQRQKELEMQLAEEQKRLMEM-AEEERLEYQQQKLAAEEKARQEaeerrKQEEEAAKLALEEAT 783
Cdd:TIGR02169 908 LEAQIEK--------KRKRLSELKAKLEALEEELSEIeDPKGEDEEIPEEELSLEDVQAE-----LQRVEEEIRALEPVN 974
|
250 260 270
....*....|....*....|....*....|..
gi 568906621 784 KLA-QEQIRQKAALDKHLHFHQELSKEASGLQ 814
Cdd:TIGR02169 975 MLAiQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
685-810 |
4.72e-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: 39.90 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 685 QAARERARQQQEELRRKLQEIQRKK--QQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQ 762
Cdd:pfam13868 19 KCNKERDAQIAEKKRIKAEEKEEERrlDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 568906621 763 EAEERRK-------QEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEA 810
Cdd:pfam13868 99 EREQMDEiveriqeEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREE 153
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
678-793 |
4.88e-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: 40.82 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 678 KKRRLQLQAARERARQQQEELRRKLQEIQRKkqqeaaeraeaEKQRQKELEMQLAEEQKRLMEMAE-EERLEYQQQKLAA 756
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRK-----------IGEIEKEIEQLEQEEEKLKERLEElEEDLSSLEQEIEN 755
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 568906621 757 EEKARQEAEER-RKQEEEAAKLALEEAT---KLAQEQIRQK 793
Cdd:TIGR02169 756 VKSELKELEARiEELEEDLHKLEEALNDleaRLSHSRIPEI 796
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
678-798 |
5.68e-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: 38.23 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 678 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraeAEKQRQKELEMQLAEEQKRLMEMAEEErleyqqqklAAE 757
Cdd:COG0711 44 ERAKEEAEAALAEYEEKLAEARAEAAEIIAEARK-------EAEAIAEEAKAEAEAEAERIIAQAEAE---------IEQ 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 568906621 758 EKARQEAEERrkqeEEAAKLALEEATKLAQEQI---RQKAALDK 798
Cdd:COG0711 108 ERAKALAELR----AEVADLAVAIAEKILGKELdaaAQAALVDR 147
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
619-794 |
5.75e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.28 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 619 KVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEaekKRRLQLQAARER-------- 690
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE---REIAELEAELERldassddl 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 691 --ARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQkelemQLAEEQKRLMEMAEE-ERLEYQQQKLAAEEKARQEAEER 767
Cdd:COG4913 688 aaLEEQLEELEAELEELEEELDELKGEIGRLEKELE-----QAEEELDELQDRLEAaEDLARLELRALLEERFAAALGDA 762
|
170 180
....*....|....*....|....*..
gi 568906621 768 RkqeEEAAKLALEEATKLAQEQIRQKA 794
Cdd:COG4913 763 V---ERELRENLEERIDALRARLNRAE 786
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
678-784 |
7.39e-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: 39.59 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 678 KKRRLQLQAARERARQQQE--------ELRRKLQEiQRKKQqeaaeraeaekQRQKELEMQLAEEQKRLMEMAEEERLEY 749
Cdd:pfam07767 209 KKRLKEEEKLERVLEKIAEsaataearEEKRKTKA-QRNKE-----------KRRKEEEREAKEEKALKKKLAQLERLKE 276
|
90 100 110
....*....|....*....|....*....|....*
gi 568906621 750 QQQKLAAEEKARQEAEERRKQEEEAAKLALEEATK 784
Cdd:pfam07767 277 IAKEIAEKEKEREEKAEARKREKRKKKKEEKKLRP 311
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
571-811 |
8.24e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 571 QATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAekmkeelel 650
Cdd:PTZ00121 1648 KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA--------- 1718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 651 EQQRRTEENRLRKQRleeerqqqeeaekkrrlQLQAARERARQQQEELRRKLQEiQRKKQQEAAERAEAEKQRQKELEMQ 730
Cdd:PTZ00121 1719 EELKKAEEENKIKAE-----------------EAKKEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAV 1780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 731 LAEEQKR---LMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELS 807
Cdd:PTZ00121 1781 IEEELDEedeKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNEN 1860
|
....
gi 568906621 808 KEAS 811
Cdd:PTZ00121 1861 GEDG 1864
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
694-810 |
8.70e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 38.84 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 694 QQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEE 773
Cdd:PRK06669 31 SIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAKEELLKKTDEASSIIEKLQMQIEREQEEWEE 110
|
90 100 110
....*....|....*....|....*....|....*..
gi 568906621 774 AAKLALEEATKLAQEQIRQKaALDKHLHFHQELSKEA 810
Cdd:PRK06669 111 ELERLIEEAKAEGYEEGYEK-GREEGLEEVRELIEQL 146
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
582-805 |
9.44e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 39.72 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 582 EEERSHEDPSKALQDKKQQEKAS-RDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQqrrTEENR 660
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHkRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQ---AELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568906621 661 LRKQRLEEERQQQeeaeKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQkelemQLAEEQKRLME 740
Cdd:pfam05557 80 LKKKYLEALNKKL----NEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQE-----RLDLLKAKASE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568906621 741 MAEE-ERLEYQQQKLAAEEKARQEAEERRKQEEEAAklaleEATKLAQEQIRQKAALDKHLHFHQE 805
Cdd:pfam05557 151 AEQLrQNLEKQQSSLAEAEQRIKELEFEIQSQEQDS-----EIVKNSKSELARIPELEKELERLRE 211
|
|
| |
