|
Name |
Accession |
Description |
Interval |
E-value |
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
588-1042 |
1.14e-127 |
|
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: 399.33 E-value: 1.14e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 588 QERGSELDSHEEPGGPLRGNAKDSQDPELRNKTLACLSTSLAEYNQPSEADTLKSMDG-DYNVHHLHRGPLKREPAFPKK 666
Cdd:pfam15709 59 KDSGEALDSHEEPGEPLGENHQDSQDPEPRSVTLSPLSASLGEHIQTPEADTVQNGDGeDYDVHHLHRGLPRHRPESPEK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 667 LA----SETPRKKKKRRS-KLLNQKTGVGINHG-KDLVDKAKRKKRTKTHQAKALKKEREERGLGQAEAAGGKPKHSKIK 740
Cdd:pfam15709 139 LTavdtSLLPRAREGKTEpRLFNQETPASISHAeRELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 741 KKSELTPKKEKLGRKMKRTHKERNMEMAAGLSKSDITNSKEAGGTSHQGLLRSHSAAGQ--LSLELDALESQVAIDGRLS 818
Cdd:pfam15709 219 KKSELISKGKKTGAKRKRTQKERNLEVAAELSGPDVINSKETEDASERGAFSSDSVVEDpwLSSKYDAEESQVSIDGRSS 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 819 SIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEEL 898
Cdd:pfam15709 299 PTQTFVVTGNMESEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREEL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 899 ELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELE 978
Cdd:pfam15709 379 ELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELE 458
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355882 979 MQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQ 1042
Cdd:pfam15709 459 MQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
799-1061 |
1.52e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.44 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 799 QLSLELDALESQVA-IDGRLSSIQATDVASDMECEEER-SHEDPSKALQDKKQQE-KASRDRIRIEKAEMRwlKVEQRRR 875
Cdd:COG1196 236 ELEAELEELEAELEeLEAELEELEAELAELEAELEELRlELEELELELEEAQAEEyELLAELARLEQDIAR--LEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 876 EQEELtwlhkEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEI 955
Cdd:COG1196 314 LEERL-----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 956 QRKKQQeaaerAEAEKQRQKELEMQLAEEQKRLmEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKL 1035
Cdd:COG1196 389 LEALRA-----AAELAAQLEELEEAEEALLERL-ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260
....*....|....*....|....*.
gi 1720355882 1036 AQEQIRQKAALDKHLHFHQELSKEAS 1061
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAE 488
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
832-1048 |
2.73e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.79 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 832 EEERSHEDPSKAlQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELtwLHKEQLEKAEKMKEELELEQQRRTEENRl 911
Cdd:PTZ00121 1572 AEEDKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK--IKAEELKKAEEEKKKVEQLKKKEAEEKK- 1647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 912 rkqrLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRklQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEM 991
Cdd:PTZ00121 1648 ----KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK--AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720355882 992 --AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLA--LEEATKLAQEQIRQKAALDK 1048
Cdd:PTZ00121 1722 kkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAhlKKEEEKKAEEIRKEKEAVIE 1782
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
847-1064 |
6.25e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 6.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 847 KKQQEKASR-----DRIRIEKAEMRWLKVEQRRREQEELtwlhKEQLEKAEKMKEELEleQQRRTEENRLRKqrleeerq 921
Cdd:COG1196 206 ERQAEKAERyrelkEELKELEAELLLLKLRELEAELEEL----EAELEELEAELEELE--AELAELEAELEE-------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 922 qqeeaekkRRLQLQAARERARQQQEELRRKLQEIQR--KKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEE----- 994
Cdd:COG1196 272 --------LRLELEELELELEEAQAEEYELLAELARleQDIARLEERRRELEERLEELEEELAELEEELEELEEEleele 343
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 995 ERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 1064
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
821-1048 |
1.72e-12 |
|
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: 71.69 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 821 QATDVASDMECEEERSHEDPSKALQDKKQQ-EKASRDRIRIEKAEMRWLKVEQRRREQEELTWlhKEQLEKAEKMKEELE 899
Cdd:pfam17380 332 QAAIYAEQERMAMERERELERIRQEERKRElERIRQEEIAMEISRMRELERLQMERQQKNERV--RQELEAARKVKILEE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 900 LEQqrRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKlQEIQRKKQQEAAERAEAEKQRQKELEM 979
Cdd:pfam17380 410 ERQ--RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQ-QQVERLRQQEEERKRKKLELEKEKRDR 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 980 QLAEEQKRLM----------EMAEEER--------LEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIR 1041
Cdd:pfam17380 487 KRAEEQRRKIlekeleerkqAMIEEERkrkllekeMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERS 566
|
....*..
gi 1720355882 1042 QKAALDK 1048
Cdd:pfam17380 567 RLEAMER 573
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
932-1045 |
1.88e-12 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 70.22 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 932 LQLQAARERARQQQEElRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKAR 1011
Cdd:PRK09510 92 LQQKQAAEQERLKQLE-KERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKK 170
|
90 100 110
....*....|....*....|....*....|....
gi 1720355882 1012 QEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1045
Cdd:PRK09510 171 AEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAE 204
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
843-1064 |
5.33e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 5.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 843 ALQDKKQQEKASRDRIRIEKAEmrwlkvEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQ 922
Cdd:COG1196 231 LLKLRELEAELEELEAELEELE------AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 923 QEEaeKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAeKQRQKELEMQLAEEQKRLMEMAEE--ERLEYQ 1000
Cdd:COG1196 305 ARL--EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA-EEELEEAEAELAEAEEALLEAEAElaEAEEEL 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355882 1001 QQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 1064
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
799-1054 |
8.08e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 8.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 799 QLSLELDALESQVAiDGRLSSIQATDVASDMECEEERSHEDPSKALQDKK-QQEKASRDRIRIEKAEMRWLKVEQRRREQ 877
Cdd:COG1196 257 ELEAELAELEAELE-ELRLELEELELELEEAQAEEYELLAELARLEQDIArLEERRRELEERLEELEEELAELEEELEEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 878 EELTwlhKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERA--RQQQEELRRKLQEI 955
Cdd:COG1196 336 EEEL---EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAelAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 956 QRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLmemAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKL 1035
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALE---EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
250
....*....|....*....
gi 1720355882 1036 AQEQIRQKAALDKHLHFHQ 1054
Cdd:COG1196 490 AARLLLLLEAEADYEGFLE 508
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
832-1064 |
1.87e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.63 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 832 EEERSHEDPSKALQDKKQQEKASRDRIR----IEKAEMRwLKVEQRRREQEELTWLHKE-----QLEKAEKMKEELELEQ 902
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKkaeeLKKAEEK-KKAEEAKKAEEDKNMALRKaeeakKAEEARIEEVMKLYEE 1603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 903 QRRTEENRLRKQRLEEERQQQ---EEAEKKRRLQLQAARERARQQQEELRRKLQEIQ------RKKQQEAAERAEAEKQR 973
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEElkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaaeeAKKAEEDKKKAEEAKKA 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 974 QKElEMQLAEEQKRlmeMAEEERLEYQQQKLAAEEKARQE----AEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKH 1049
Cdd:PTZ00121 1684 EED-EKKAAEALKK---EAEEAKKAEELKKKEAEEKKKAEelkkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
|
250
....*....|....*
gi 1720355882 1050 LHFHQELSKEASGLQ 1064
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIR 1774
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
936-1060 |
2.13e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 67.14 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 936 AARERARQQQEELRRKLQEIQRKKQQeaaeraeaeKQRQKELEMQLAEEQKRLMEMaEEERLEYQQQKLAAEEKARQEAE 1015
Cdd:PRK09510 60 VVEQYNRQQQQQKSAKRAEEQRKKKE---------QQQAEELQQKQAAEQERLKQL-EKERLAAQEQKKQAEEAAKQAAL 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355882 1016 ERRKQEEEAAKLA-------------LEEATKLAQEQIRQKAALDKHLHFHQELSKEA 1060
Cdd:PRK09510 130 KQKQAEEAAAKAAaaakakaeaeakrAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKA 187
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
842-1064 |
2.61e-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: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 842 KALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEE-NRLRKqrleeer 920
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELElEEAQA------- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 921 qqQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQR-QKELEMQLAEEQKRLMEMAEEERLEY 999
Cdd:COG1196 289 --EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELeELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720355882 1000 QQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 1064
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
928-1048 |
9.54e-11 |
|
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: 64.87 E-value: 9.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 928 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEyQQQKLAAE 1007
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE-AKAKQAAE 131
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1720355882 1008 EKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDK 1048
Cdd:TIGR02794 132 AKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAK 172
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
842-1033 |
2.31e-10 |
|
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: 64.76 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 842 KALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEqleKAEKMKEELELEQQRRTEENRLRKQRLEEERQ 921
Cdd:pfam17380 399 EAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEE---RAREMERVRLEEQERQQQVERLRQQEEERKRK 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 922 QQEEAEKKRRLQLQAARERA--RQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEY 999
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKilEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720355882 1000 QQQKLAAEEKARQEAEERRKQ------EEEAAKLALEEAT 1033
Cdd:pfam17380 556 EQMRKATEERSRLEAMEREREmmrqivESEKARAEYEATT 595
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
832-1048 |
2.48e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 65.16 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 832 EEERSHEDPSKAlQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQL----EKAEKMKEELELEQQRRTE 907
Cdd:PTZ00121 1215 EEARKAEDAKKA-EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaikaEEARKADELKKAEEKKKAD 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 908 ENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKR 987
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK 1373
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355882 988 LMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEE-----AAKLALEEATKLAQEQIRQKAALDK 1048
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADElkkaaAAKKKADEAKKKAEEKKKADEAKKK 1439
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
832-1044 |
7.02e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 7.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 832 EEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENR- 910
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKk 1553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 911 ---LRKQRLEEERQQQEEAEKKRRLQLQAARE--RARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMqlAEEQ 985
Cdd:PTZ00121 1554 aeeLKKAEEKKKAEEAKKAEEDKNMALRKAEEakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK--AEEE 1631
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 986 KRLMEM-----------AEEERLEYQQQKLAAEEKARQEAEERRKQEEeaAKLAlEEATKLAQEQIRQKA 1044
Cdd:PTZ00121 1632 KKKVEQlkkkeaeekkkAEELKKAEEENKIKAAEEAKKAEEDKKKAEE--AKKA-EEDEKKAAEALKKEA 1698
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
935-1060 |
9.53e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 58.32 E-value: 9.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 935 QAARERARQQQEELRRKLQEIQRKKQQeaaeraeaeKQRQKELEMQLAEEQKRLMEM-----AEEERLEYQQQKLAAEEK 1009
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKL---------EQQAEEAEKQRAAEQARQKELeqraaAEKAAKQAEQAAKQAEEK 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1720355882 1010 ARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEA 1060
Cdd:TIGR02794 118 QKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKA 168
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
829-1048 |
1.44e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 829 MECEEERSHEDPSKALQDKKQQEKASRDRIRieKAEMRWLKVEQRRREQEEltwlhKEQLEKAEKMKEELELEQQRRTEE 908
Cdd:PTZ00121 1272 IKAEEARKADELKKAEEKKKADEAKKAEEKK--KADEAKKKAEEAKKADEA-----KKKAEEAKKKADAAKKKAEEAKKA 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 909 NRLRKQRLEEERQQQEEAEKKRRLQlQAARERARQQQEELRRKLQEIqrKKQQEAAERAEAEKQRQKELEMQLAEEQK-- 986
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEAA-EKKKEEAKKKADAAKKKAEEK--KKADEAKKKAEEDKKKADELKKAAAAKKKad 1421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720355882 987 RLMEMAEEERLEYQQQKLAAE----EKARQEAEERRKQEE-----EAAKLAlEEATKLAQEQIRQKAALDK 1048
Cdd:PTZ00121 1422 EAKKKAEEKKKADEAKKKAEEakkaDEAKKKAEEAKKAEEakkkaEEAKKA-DEAKKKAEEAKKADEAKKK 1491
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
842-1042 |
2.17e-08 |
|
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: 58.21 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 842 KALQDKKQQEKASR---DRIRIEKAEmRWLKVEQRRR--------------------EQEELTWLHKEQLEKAEKMKEEL 898
Cdd:pfam17380 282 KAVSERQQQEKFEKmeqERLRQEKEE-KAREVERRRKleeaekarqaemdrqaaiyaEQERMAMERERELERIRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 899 ELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRL--QLQAAReRARQQQEELRRKLQEIQRKKQQeaaERAEAEKQRQKE 976
Cdd:pfam17380 361 ELERIRQEEIAMEISRMRELERLQMERQQKNERVrqELEAAR-KVKILEEERQRKIQQQKVEMEQ---IRAEQEEARQRE 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355882 977 LEmQLAEEQKRLMEMAEEERLEYQQQKlaaeEKARQEAEERRKQEEEAAKlaLEEATKLAQEQIRQ 1042
Cdd:pfam17380 437 VR-RLEEERAREMERVRLEEQERQQQV----ERLRQQEEERKRKKLELEK--EKRDRKRAEEQRRK 495
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
800-1078 |
2.22e-08 |
|
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: 58.54 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 800 LSLELDALESQ-VAIDGRLSSIQA--TDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQR--R 874
Cdd:TIGR02169 228 LLKEKEALERQkEAIERQLASLEEelEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAslE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 875 REQEELtwlhKEQLEKAEKmkeeleleQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQE 954
Cdd:TIGR02169 308 RSIAEK----ERELEDAEE--------RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 955 IQRKKQqeaaERAEAEKQRQKELEM------QLAEEQKRLMEMAE---------EERLEYQQQKLAAEEKARQEAEERRK 1019
Cdd:TIGR02169 376 VDKEFA----ETRDELKDYREKLEKlkreinELKRELDRLQEELQrlseeladlNAAIAGIEAKINELEEEKEDKALEIK 451
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355882 1020 QEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQWTQNISRPWVYSYF 1078
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
711-1058 |
3.01e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 3.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 711 QAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELTPKKEKLGRKMKRTHKERNMEMAAGLSKSDITNSKEAGGTSHQGL 790
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 791 LRSHSAAGQLSLELDALESQVAIDGRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKV 870
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 871 EQRRREQEELTwlhKEQLEKAEKMKEELELEQQRRTEENRLR---KQRLEEERQQQEEAEKKRRLQLQAARERarqQQEE 947
Cdd:PTZ00121 1401 EEDKKKADELK---KAAAAKKKADEAKKKAEEKKKADEAKKKaeeAKKADEAKKKAEEAKKAEEAKKKAEEAK---KADE 1474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 948 LRRKLQEIQRK---KQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKarQEAEERRKQEE-- 1022
Cdd:PTZ00121 1475 AKKKAEEAKKAdeaKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA--KKAEEKKKADElk 1552
|
330 340 350
....*....|....*....|....*....|....*.
gi 1720355882 1023 EAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSK 1058
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
782-1039 |
7.05e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 782 AGGTSHQGLLRSHSAAGQLSLELDALESQVAI---DGRLSSIQATDVasdmeceeERSHEDPSKALQDKKQQEKASRDRI 858
Cdd:TIGR02168 657 PGGVITGGSAKTNSSILERRREIEELEEKIEEleeKIAELEKALAEL--------RKELEELEEELEQLRKELEELSRQI 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 859 RIEKAEMRWLKVEQRRREQEeltwlhKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAAR 938
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEER------IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 939 ERARQQQEELRRKLQEIQRK--KQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEerLEYQQQKLAAEEKARQEAEE 1016
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAE--IEELEELIEELESELEALLN 880
|
250 260
....*....|....*....|...
gi 1720355882 1017 RRKQEEEAAKLALEEATKLAQEQ 1039
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEEL 903
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
935-1045 |
1.18e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 55.65 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 935 QAARERARQQQEELRRklQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLmEMAEEERLEyQQQKLAAEEKARQEA 1014
Cdd:COG2268 241 EAEAELAKKKAEERRE--AETARAEAEAAYEIAEANAEREVQRQLEIAEREREI-ELQEKEAER-EEAELEADVRKPAEA 316
|
90 100 110
....*....|....*....|....*....|..
gi 1720355882 1015 EERRKQEEEAAKLALEEATKLAQ-EQIRQKAA 1045
Cdd:COG2268 317 EKQAAEAEAEAEAEAIRAKGLAEaEGKRALAE 348
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
838-1048 |
1.61e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 54.88 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 838 EDPSKAL--QDKKQQEKASRDRiRIEKAEMRW---LKVEQRRREQEEltwlhkEQLEKAEKMKEELELEQQRRTEEnrlr 912
Cdd:COG2268 180 EDENNYLdaLGRRKIAEIIRDA-RIAEAEAEReteIAIAQANREAEE------AELEQEREIETARIAEAEAELAK---- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 913 kqrleeerqqqeeaeKKRRLQLQAARERARQQQE-ELRR--KLQEIQRKKQQEaaeraeaekQRQKELEMQLAEEQKRLM 989
Cdd:COG2268 249 ---------------KKAEERREAETARAEAEAAyEIAEanAEREVQRQLEIA---------EREREIELQEKEAEREEA 304
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720355882 990 EMAEEERLEYQQQKLAAEEKARQEAE-ERRKQEEEA-AKLALEEATKLAQEQIRQKAALDK 1048
Cdd:COG2268 305 ELEADVRKPAEAEKQAAEAEAEAEAEaIRAKGLAEAeGKRALAEAWNKLGDAAILLMLIEK 365
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
834-1045 |
3.69e-07 |
|
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: 53.38 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 834 ERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRK 913
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 914 qrleeerqqqeeaekkRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEM------QLAEEQKR 987
Cdd:pfam13868 188 ----------------RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELqqareeQIELKERR 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355882 988 LMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLAlEEATKLAQEQIRQKAA 1045
Cdd:pfam13868 252 LAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHR-RELEKQIEEREEQRAA 308
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
905-1060 |
5.86e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 5.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 905 RTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQ-EAAERAEAEKQRQKELEMQLAE 983
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355882 984 EQKRLMEMaeEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEA 1060
Cdd:COG4717 144 LPERLEEL--EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
832-1048 |
1.09e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 832 EEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRwlKVEQRRrEQEELTWLHKEQLEKAEKMKEELELEQQRRTEEnrL 911
Cdd:PTZ00121 1209 EEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK--KAEEER-NNEEIRKFEEARMAHFARRQAAIKAEEARKADE--L 1283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 912 RKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAEraeaekqrqkelemqlAEEQKRLMEM 991
Cdd:PTZ00121 1284 KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKK----------------AEEAKKAAEA 1347
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355882 992 AEEERLEYQQQKLAAEEKArqEAEERRKQEEeaaKLALEEATKLAQE-----QIRQKAALDK 1048
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKA--EAAEKKKEEA---KKKADAAKKKAEEkkkadEAKKKAEEDK 1404
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
845-1045 |
1.28e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.18 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 845 QDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQE 924
Cdd:pfam02029 143 NKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVT 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 925 EAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRlmemAEEERleyqqqkl 1004
Cdd:pfam02029 223 TKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKK----REERR-------- 290
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720355882 1005 aaeeKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1045
Cdd:pfam02029 291 ----KLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERRRA 327
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
939-1028 |
1.51e-06 |
|
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: 48.88 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 939 ERARQQQEELRRKLQEiQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEY-QQQKLAAEEKARQEAE-- 1015
Cdd:pfam05672 39 EEERLRKEELRRRAEE-ERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERlQKQKEEAEAKAREEAErq 117
|
90
....*....|....*..
gi 1720355882 1016 ----ERRKQEEEAAKLA 1028
Cdd:pfam05672 118 rqerEKIMQQEEQERLE 134
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
844-1059 |
2.01e-06 |
|
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: 51.07 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 844 LQDKKQQEKASRDRIRIEKAEMRwlkvEQRRREQEELtwLHKEQLEKAEKMKEELELEQQRrtEENRLRKQRLEEERQQQ 923
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMME----EERERALEEE--EEKEEERKEERKRYRQELEEQI--EEREQKRQEEYEEKLQE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 924 EEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAE-----EQKRLMEMAEEERLE 998
Cdd:pfam13868 100 REQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEylkekAEREEEREAEREEIE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720355882 999 YQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKE 1059
Cdd:pfam13868 180 EEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQA 240
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
819-1031 |
2.14e-06 |
|
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: 51.07 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 819 SIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEmrwlkveQRRREQEELTwlhkEQLEKAEKMKEEL 898
Cdd:pfam13868 135 FNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEE-------EKEREIARLR----AQQEKAQDEKAER 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 899 ELEQQRRTEENRLRKQRLEEERQQQeeaeKKRRLQLQAARERARQQQEELRRKLQEIQR---------KKQQEAAERAEA 969
Cdd:pfam13868 204 DELRAKLYQEEQERKERQKEREEAE----KKARQRQELQQAREEQIELKERRLAEEAEReeeefermlRKQAEDEEIEQE 279
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355882 970 EKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEE 1031
Cdd:pfam13868 280 EAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
788-1038 |
2.25e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 788 QGLLRSHSAAGQLSLELDALESQVAidgRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRdRIRIEKAEMRW 867
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELA---ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA-LLEAEAELAEA 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 868 LKVEQRRREQEEltwlhkeQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEE 947
Cdd:COG1196 378 EEELEELAEELL-------EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 948 LRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKL 1027
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
|
250
....*....|.
gi 1720355882 1028 ALEEATKLAQE 1038
Cdd:COG1196 531 GVEAAYEAALE 541
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
842-1038 |
2.30e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.70 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 842 KALQDKKQQEKASRDRIrIEKAEMrwlKVEQRRRE-----QEELTWLhKEQLEKAEKMKEELELEQQRRTE--ENRLRKQ 914
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRI-LEEAKK---EAEAIKKEalleaKEEIHKL-RNEFEKELRERRNELQKLEKRLLqkEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 915 RLEEerqqqeeaeKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraeaekqRQKELE--MQLAEEQ--KRLME 990
Cdd:PRK12704 102 LELL---------EKREEELEKKEKELEQKQQELEKKEEELEELIEE-----------QLQELEriSGLTAEEakEILLE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720355882 991 MAEEErleyqqqklaaeekARQEAEERRKQEEEAAKlalEEATKLAQE 1038
Cdd:PRK12704 162 KVEEE--------------ARHEAAVLIKEIEEEAK---EEADKKAKE 192
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
928-1059 |
2.94e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 928 KKRRLQLQAARERARQQQE-ELRRKLQEIQRKKQQEaaeraeaeKQRQKELEMQLAEEQKRlmemaeEERLEYQQQKLAA 1006
Cdd:PRK12704 56 KEALLEAKEEIHKLRNEFEkELRERRNELQKLEKRL--------LQKEENLDRKLELLEKR------EEELEKKEKELEQ 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355882 1007 E----EKARQEAEERRKQE----EEAAKLALEEATKLAQEQIRQKAALDKHLHFHQ--ELSKE 1059
Cdd:PRK12704 122 KqqelEKKEEELEELIEEQlqelERISGLTAEEAKEILLEKVEEEARHEAAVLIKEieEEAKE 184
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
799-1036 |
3.08e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 799 QLSLELDALESQVAI-DGRLSSIQATDVASDMECEEERSHEDPSKA----LQDKKQQEKASRDRIRIEKAEMRWLKVEQR 873
Cdd:TIGR02168 292 ALANEISRLEQQKQIlRERLANLERQLEELEAQLEELESKLDELAEelaeLEEKLEELKEELESLEAELEELEAELEELE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 874 RREQEEltwlhKEQLEKAEKMKEELEleQQRRTEENRLRkqrleeerqqqeeAEKKRRLQLQAARERARQQQEELRRKLQ 953
Cdd:TIGR02168 372 SRLEEL-----EEQLETLRSKVAQLE--LQIASLNNEIE-------------RLEARLERLEDRRERLQQEIEELLKKLE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 954 EIQRKKQQEA----AERAEAEKQRQKELEMQLAEEQKRLMEMAEEER-LEYQQQKLAAEEKARQEAEERRKQEEEAAKLA 1028
Cdd:TIGR02168 432 EAELKELQAEleelEEELEELQEELERLEEALEELREELEEAEQALDaAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
....*...
gi 1720355882 1029 LEEATKLA 1036
Cdd:TIGR02168 512 LKNQSGLS 519
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
847-1064 |
3.30e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 847 KKQQEKASRDR-IRIEKAEMRW----LKVEQRRREQEELtwlhKEQLEKAEKMKEELELEQQRRTEE-NRLRKQrleeer 920
Cdd:TIGR02168 206 ERQAEKAERYKeLKAELRELELallvLRLEELREELEEL----QEELKEAEEELEELTAELQELEEKlEELRLE------ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 921 qqqEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraeaEKQRQKELEMQLAEEQKRLMEMAEE-ERLEY 999
Cdd:TIGR02168 276 ---VSELEEEIEELQKELYALANEISRLEQQKQILRERLAN--------LERQLEELEAQLEELESKLDELAEElAELEE 344
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355882 1000 QQQKLAAE--------EKARQEAEERRKQEEEAAKLALEEATKLAQEQiRQKAALDKHLhfhQELSKEASGLQ 1064
Cdd:TIGR02168 345 KLEELKEElesleaelEELEAELEELESRLEELEEQLETLRSKVAQLE-LQIASLNNEI---ERLEARLERLE 413
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
830-1015 |
3.32e-06 |
|
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: 51.28 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 830 ECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKaekmkeeLELEQQRRTEEN 909
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEK-------EKRDRKRAEEQR 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 910 R-LRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraEAEKQRQKELEMQLAEEQKRL 988
Cdd:pfam17380 494 RkILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQ------EMEERRRIQEQMRKATEERSR 567
|
170 180
....*....|....*....|....*..
gi 1720355882 989 MEMAEEERLEYQQqkLAAEEKARQEAE 1015
Cdd:pfam17380 568 LEAMEREREMMRQ--IVESEKARAEYE 592
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
832-1029 |
3.58e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 832 EEERSHEDPSKALQDKKQQEKASRDRIRIEKAEmrwLKVEQRRREQEELTWLHKEQLEKAEkmkeeleleQQRRTEENRL 911
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEE---LREELEKLEKLLQLLPLYQELEALE---------AELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 912 RKQRLEEerqqqeeaekKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEm 991
Cdd:COG4717 149 EELEERL----------EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE- 217
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720355882 992 aEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLAL 1029
Cdd:COG4717 218 -AQEELEELEEELEQLENELEAAALEERLKEARLLLLI 254
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
871-1048 |
3.88e-06 |
|
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: 50.23 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 871 EQRRREQEELtwlhkEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRR 950
Cdd:TIGR02794 61 PAAKKEQERQ-----KKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 951 KLQEIQRKKQQEAaeraeaEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEaEERRKQEEEAAKLALE 1030
Cdd:TIGR02794 136 AEAEAERKAKEEA------AKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAE-EAKAKAEAAKAKAAAE 208
|
170
....*....|....*...
gi 1720355882 1031 EATKLAQEQIRQKAALDK 1048
Cdd:TIGR02794 209 AAAKAEAEAAAAAAAEAE 226
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
842-1046 |
4.18e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 842 KALQDKKQQ-EKASRDRIRIEKAEMRWL--KVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEE 918
Cdd:COG4717 49 ERLEKEADElFKPQGRKPELNLKELKELeeELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 919 ERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaerAEAEKQRQKELEMQLAEEQKRLMEMAEEERLE 998
Cdd:COG4717 129 PLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE-----LAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720355882 999 YQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAAL 1046
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
842-1052 |
4.39e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 842 KALQDKKQQEKASRDRIR--IEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEE--NRLRKQRLE 917
Cdd:COG4942 37 AELEKELAALKKEEKALLkqLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElaELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 918 EERQQQE-------EAEKKRRLQLQAARERARQQQ-EELRRKLQEIQRKKQQeaaerAEAEKQRQKELEMQLAEEQKRLm 989
Cdd:COG4942 117 GRQPPLAlllspedFLDAVRRLQYLKYLAPARREQaEELRADLAELAALRAE-----LEAERAELEALLAELEEERAAL- 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355882 990 emaeeERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHF 1052
Cdd:COG4942 191 -----EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
832-1041 |
8.57e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 8.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 832 EEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEEltwlHKEQLE-KAEKMKEELELEQQRRTEENR 910
Cdd:TIGR02169 204 RREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE----ELEKLTeEISELEKRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 911 lrkqRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeAAERAEAEKQRQKELEMQLAEEQKRLME 990
Cdd:TIGR02169 280 ----KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK-LEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355882 991 MAEE-----ERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIR 1041
Cdd:TIGR02169 355 LTEEyaelkEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
933-1045 |
9.94e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 9.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 933 QLQAARERARQQQEELRRKLQEIQRKKQQEaaeraeaeKQRQKELEMQLAEEQKRLMEMAEEERlEYQQQKlAAEEKARQ 1012
Cdd:COG3883 137 ELKADKAELEAKKAELEAKLAELEALKAEL--------EAAKAELEAQQAEQEALLAQLSAEEA-AAEAQL-AELEAELA 206
|
90 100 110
....*....|....*....|....*....|...
gi 1720355882 1013 EAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1045
Cdd:COG3883 207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
839-1048 |
1.03e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 839 DPSKALQD--KKQQEKASRDRirieKAEMRWLKVEQRRREQEEltwlhkEQLEkaekmkeeleleQQRRTEENRLRKQRL 916
Cdd:PRK09510 56 DPGAVVEQynRQQQQQKSAKR----AEEQRKKKEQQQAEELQQ------KQAA------------EQERLKQLEKERLAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 917 EEERQQQEEAEKKRRLQLQAARERARQQQEElrrklqeiqrkkqqeaaeraeaEKQRQKELEMQLAEEQKRLMEMAEEER 996
Cdd:PRK09510 114 QEQKKQAEEAAKQAALKQKQAEEAAAKAAAA----------------------AKAKAEAEAKRAAAAAKKAAAEAKKKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1720355882 997 LEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDK 1048
Cdd:PRK09510 172 EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEA 223
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
928-1055 |
1.60e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 48.94 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 928 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAE-----EERLEYQQQ 1002
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEkldnlENQLEEREK 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355882 1003 KLAAEEKARQEAEERRKQE-EEAAKLALEEATKL--------AQEQIRQKAALDKH-LHFHQE 1055
Cdd:PRK12705 113 ALSARELELEELEKQLDNElYRVAGLTPEQARKLllklldaeLEEEKAQRVKKIEEeADLEAE 175
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
871-1048 |
1.99e-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: 48.81 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 871 EQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQL--QAARERARQQQEEL 948
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLdyLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 949 RRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLA 1028
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180
....*....|....*....|
gi 1720355882 1029 LEEATKLAQEQIRQKAALDK 1048
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELK 345
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
849-1059 |
2.12e-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: 48.58 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 849 QQEKASRDRIRIEKAEmrwlKVEQRRREQEeltwlhKEQLEKaekmkeelelEQQRRTEENRLRKQRLEEERQQQEEAEK 928
Cdd:pfam17380 279 QHQKAVSERQQQEKFE----KMEQERLRQE------KEEKAR----------EVERRRKLEEAEKARQAEMDRQAAIYAE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 929 KRRLQLQAARERARQQQEELRRKLQEI----------------------QRKKQQEAAERAEAEKQRQKELEMQ-LAEEQ 985
Cdd:pfam17380 339 QERMAMERERELERIRQEERKRELERIrqeeiameisrmrelerlqmerQQKNERVRQELEAARKVKILEEERQrKIQQQ 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355882 986 KRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKE 1059
Cdd:pfam17380 419 KVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ 492
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
902-1050 |
3.01e-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: 48.08 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 902 QQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKqrqkelemQL 981
Cdd:pfam05262 204 KERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDK--------QV 275
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355882 982 AEEQKRLMEMAEEE----RLEYQQQKLAAEEKARQEA---EERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHL 1050
Cdd:pfam05262 276 AENQKREIEKAQIEikknDEEALKAKDHKAFDLKQESkasEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSL 351
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
939-1042 |
5.35e-05 |
|
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: 44.65 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 939 ERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERR 1018
Cdd:pfam05672 10 EEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEERE 89
|
90 100 110
....*....|....*....|....*....|....*
gi 1720355882 1019 -----------KQEEEAAKLALEEATKLAQEQIRQ 1042
Cdd:pfam05672 90 qreqeeqerlqKQKEEAEAKAREEAERQRQEREKI 124
|
|
| DDRGK |
pfam09756 |
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ... |
950-1024 |
6.06e-05 |
|
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: 45.03 E-value: 6.06e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355882 950 RKLQEIQRKKQQEAAEraeaeKQRQKELEMQLAEEQKRLMEMAEEERLEYQ-QQKLAAEEKARQEA---EERRKQEEEA 1024
Cdd:pfam09756 1 KKLGAKKRAKLELKEA-----KRQQREAEEEEREEREKLEEKREEEYKEREeREEEAEKEKEEEERkqeEEQERKEQEE 74
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
817-1059 |
6.40e-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: 47.27 E-value: 6.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 817 LSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKV-EQRRREQEELTWLHKEQLEKAEKMK 895
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERrKVDDEEKLKESEKEKKKAEKELKKE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 896 EELELEQQRRTEENRLRKQRLEEERQQqeeaekkrrlqlqaarerARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQK 975
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAEEEEEEE------------------LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 976 ELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEaAKLALEEATKLAQEQIRQKAALDKHLHFHQE 1055
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ-GKLTEEKEELEKQELKLLKDELELKKSEDLL 474
|
....
gi 1720355882 1056 LSKE 1059
Cdd:pfam02463 475 KETQ 478
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
787-1068 |
7.08e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 7.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 787 HQGLLRSHSAAGQLSLELDALESQV-AIDGRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQekasrdRIRIEKAEM 865
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELqELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ------QKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 866 RWLKVEQRRREqeeltwlhkEQLEKAEkmkeELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQ 945
Cdd:TIGR02168 312 ANLERQLEELE---------AQLEELE----SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 946 EELRRKLQEIQRKKQQEAAERAeaekqRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAA 1025
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNN-----EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ 453
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1720355882 1026 K--LALEEATKLAQEQIRQK-AALDKHLHFHQELSKEASGLQWTQN 1068
Cdd:TIGR02168 454 EelERLEEALEELREELEEAeQALDAAERELAQLQARLDSLERLQE 499
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
711-1045 |
8.34e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 711 QAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELtpkKEKLGRKMKRTHKERNMEMAAGLSKSDITNSKEAGGTshQGL 790
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAEL---LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL--RGL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 791 LRSHSAAGQLSLELDALEsQVAIDGRLSSIQATDVASDMECEEERSHEDPSKA----LQDKKQQEKASRDRIRIEKAEMR 866
Cdd:COG1196 523 AGAVAVLIGVEAAYEAAL-EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflpLDKIRARAALAAALARGAIGAAV 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 867 WLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLR-KQRLEEERQQQEEAEKKRRLQLQAARERARQQQ 945
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLReVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 946 EELRRKLQEIQRKKQQeaaeraeaeKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAA 1025
Cdd:COG1196 682 EELAERLAEEELELEE---------ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
330 340
....*....|....*....|
gi 1720355882 1026 KLALEEATKLAQEQIRQKAA 1045
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 ... |
799-1033 |
8.75e-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: 46.89 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 799 QLSLELDALESQVaidgrLSSIQATDVASDMECEEERSHEDPSKaLQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQE 878
Cdd:pfam02463 268 AQVLKENKEEEKE-----KKLQEEELKLLAKEEEELKSELLKLE-RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 879 ELTWLHKEQLEKAEKMKEEleLEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAAR----ERARQQQEELRRKLQE 954
Cdd:pfam02463 342 KELKELEIKREAEEEEEEE--LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELkseeEKEAQLLLELARQLED 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 955 IQRKKQQEAAERAEAEKQRQKELEMQLAEEQ-KRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEAT 1033
Cdd:pfam02463 420 LLKEEKKEELEILEEEEESIELKQGKLTEEKeELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERS 499
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
933-1057 |
9.27e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.59 E-value: 9.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 933 QLQAARERAR----------QQQEELRRKLQEIQRKKQ----------QEAAERAEAEKQRQK----ELEM-QL-AEEQK 986
Cdd:PRK10929 124 QAQQEQDRAReisdslsqlpQQQTEARRQLNEIERRLQtlgtpntplaQAQLTALQAESAALKalvdELELaQLsANNRQ 203
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355882 987 RLMEMAEE------ERLEYQQQKLaaeekaRQEAEERRKQEeeaAKLALEEATKLAQEQIRQKAALDKHLHFHQELS 1057
Cdd:PRK10929 204 ELARLRSElakkrsQQLDAYLQAL------RNQLNSQRQRE---AERALESTELLAEQSGDLPKSIVAQFKINRELS 271
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
830-1060 |
9.69e-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: 9.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 830 ECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEEN 909
Cdd:pfam02463 195 LKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKEN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 910 RLRKQRLEEERQQQEEAEKKRRlQLQAARERARQQQEELRRKLQEIQR---------KKQQEAAERAEAEKQRQ--KELE 978
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEE-ELKSELLKLERRKVDDEEKLKESEKekkkaekelKKEKEEIEELEKELKELeiKREA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 979 MQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRkqEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSK 1058
Cdd:pfam02463 354 EEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK--EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEI 431
|
..
gi 1720355882 1059 EA 1060
Cdd:pfam02463 432 LE 433
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
928-1059 |
1.20e-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: 46.00 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 928 KKRRLQLQAARerarQQQEELRRKL-----------QEIQRKKQ-----QEAAERAEAEKQRQKE--------------- 976
Cdd:pfam09726 405 KKLKAELQASR----QTEQELRSQIssltslerslkSELGQLRQendllQTKLHNAVSAKQKDKQtvqqlekrlkaeqea 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 977 ---LEMQLAEEQKRLMEmaEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFH 1053
Cdd:pfam09726 481 rasAEKQLAEEKKRKKE--EEATAARAVALAAASRGECTESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQELRKY 558
|
....*.
gi 1720355882 1054 QELSKE 1059
Cdd:pfam09726 559 KESEKD 564
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
929-1027 |
1.20e-04 |
|
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: 42.60 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 929 KRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEyqQQKLAAEE 1008
Cdd:pfam20492 13 ERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLE--AELAEAQE 90
|
90
....*....|....*....
gi 1720355882 1009 KARQEAEERRKQEEEAAKL 1027
Cdd:pfam20492 91 EIARLEEEVERKEEEARRL 109
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
847-1071 |
1.26e-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: 46.37 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 847 KKQQEKASRDRIRIEKAEMRWLK-----VEQRRREQEELTwLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQ 921
Cdd:pfam12128 311 SAADAAVAKDRSELEALEDQHGAfldadIETAAADQEQLP-SWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNN 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 922 QQEEAEKKRRlqlQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLME-MAEEERLEYQ 1000
Cdd:pfam12128 390 RDIAGIKDKL---AKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQaTATPELLLQL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 1001 QQKLAAEEKARQEAEERRKQ------EEEAAKLALEEAT-KLAQEQIR---QKAALDKHLH--------FHQELSKEASG 1062
Cdd:pfam12128 467 ENFDERIERAREEQEAANAEverlqsELRQARKRRDQASeALRQASRRleeRQSALDELELqlfpqagtLLHFLRKEAPD 546
|
....*....
gi 1720355882 1063 lqWTQNISR 1071
Cdd:pfam12128 547 --WEQSIGK 553
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
971-1045 |
1.37e-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: 42.81 E-value: 1.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355882 971 KQRQKELEMQLAEEQKRLMEM---AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1045
Cdd:cd06503 43 EKAKEEAEELLAEYEEKLAEAraeAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVA 120
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
928-1045 |
1.64e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.42 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 928 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAE 1007
Cdd:COG3064 44 LAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAE 123
|
90 100 110
....*....|....*....|....*....|....*...
gi 1720355882 1008 EKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1045
Cdd:COG3064 124 EAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAA 161
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
935-1060 |
1.76e-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: 44.91 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 935 QAARERARQQQEELRRKLQEIQRKK--QQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQ 1012
Cdd:pfam13868 19 KCNKERDAQIAEKKRIKAEEKEEERrlDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1720355882 1013 EAEERRK-------QEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEA 1060
Cdd:pfam13868 99 EREQMDEiveriqeEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREE 153
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
784-1036 |
1.84e-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: 45.73 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 784 GTSHQGLLRSHSAAGQLSLELDALESQvaidgRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKA 863
Cdd:TIGR00618 152 GEFAQFLKAKSKEKKELLMNLFPLDQY-----TQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEK 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 864 EMRWLKVEQRRREQEEltWLHKEQLEKAEKMKEELELEQQRRTEENRLR---KQRLEEERQQQEEAEKKRRLQLQAARER 940
Cdd:TIGR00618 227 ELKHLREALQQTQQSH--AYLTQKREAQEEQLKKQQLLKQLRARIEELRaqeAVLEETQERINRARKAAPLAAHIKAVTQ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 941 ARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQkrLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQ 1020
Cdd:TIGR00618 305 IEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT--LHSQEIHIRDAHEVATSIREISCQQHTLTQHIH 382
|
250
....*....|....*.
gi 1720355882 1021 EEEAAKLALEEATKLA 1036
Cdd:TIGR00618 383 TLQQQKTTLTQKLQSL 398
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
794-1050 |
2.14e-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: 45.34 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 794 HSAAGQLSLELDALESQVAIDGRLSSIQATDVASDMECE--EERSHEDPSKALQDKKQQEKasrDRIRIEKAEMRWLKVE 871
Cdd:TIGR00618 416 TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEklEKIHLQESAQSLKEREQQLQ---TKEQIHLQETRKKAVV 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 872 -QRRREQEELTWLHKEQLekaekMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRR 950
Cdd:TIGR00618 493 lARLLELQEEPCPLCGSC-----IHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQE 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 951 KLQEIQRKKQQEAAERAEAEKQRQKELEMQ-LAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEA-AKLA 1028
Cdd:TIGR00618 568 IQQSFSILTQCDNRSKEDIPNLQNITVRLQdLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAlKLTA 647
|
250 260
....*....|....*....|...
gi 1720355882 1029 LE-EATKLAQEQIRQKAALDKHL 1050
Cdd:TIGR00618 648 LHaLQLTLTQERVREHALSIRVL 670
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
851-1064 |
2.29e-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: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 851 EKASRDRIRIEKAEMRWLK-----VEQRRREQEELTWL--HKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQ 923
Cdd:COG4913 220 EPDTFEAADALVEHFDDLEraheaLEDAREQIELLEPIreLAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 924 EEAEKKRrlqLQAARERARQQQEELRRKLQEIQRKKQQEAAeraeaekQRQKELEMQLAEEQKRLMEmAEEERLEYQQQK 1003
Cdd:COG4913 300 LRAELAR---LEAELERLEARLDALREELDELEAQIRGNGG-------DRLEQLEREIERLERELEE-RERRRARLEALL 368
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355882 1004 LAAEEKARQEAEE--RRKQEEEAAKLALEEATKLAQEQIRQ-KAALDKHLHFHQELSKEASGLQ 1064
Cdd:COG4913 369 AALGLPLPASAEEfaALRAEAAALLEALEEELEALEEALAEaEAALRDLRRELRELEAEIASLE 432
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
971-1045 |
3.37e-04 |
|
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: 42.08 E-value: 3.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355882 971 KQRQKELEMQLAEEQKRLMEM---AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1045
Cdd:COG0711 44 ERAKEEAEAALAEYEEKLAEAraeAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVA 121
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
829-1043 |
3.79e-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: 44.14 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 829 MECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRwLKVEQRRREQEELTWLHKEQLEKaekmkeelelEQQRRTEE 908
Cdd:pfam13868 82 IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAE-EKLEKQRQLREEIDEFNEEQAEW----------KELEKEEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 909 NRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQeELRRKLQEIQRKKQQE----AAERAEAEKQRQKELEMQLAEE 984
Cdd:pfam13868 151 REEDERILEYLKEKAEREEEREAEREEIEEEKEREIA-RLRAQQEKAQDEKAERdelrAKLYQEEQERKERQKEREEAEK 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355882 985 QKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQK 1043
Cdd:pfam13868 230 KARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKR 288
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
922-1026 |
4.55e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.91 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 922 QQEEAEKKRRLQLQAARERARQQQEELRRKLQEiQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEM-AEEERLEYQ 1000
Cdd:PRK11637 170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYE-QQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELrANESRLRDS 248
|
90 100 110
....*....|....*....|....*....|.
gi 1720355882 1001 QQKLAAEEKARQEAEER-----RKQEEEAAK 1026
Cdd:PRK11637 249 IARAEREAKARAEREAReaarvRDKQKQAKR 279
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
832-1064 |
5.09e-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: 44.28 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 832 EEERSHEdpsKALQ-DKKQQEKASRDRIRIEKAEMrwlkVEQRRREQEELTWLHK--EQLEKAEKMKEELELEQQRRTEE 908
Cdd:TIGR02168 220 AELRELE---LALLvLRLEELREELEELQEELKEA----EEELEELTAELQELEEklEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 909 NRLRKQRLEEERqqqeEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKqqeaaeraeaeKQRQKELEmQLAEEQKRL 988
Cdd:TIGR02168 293 LANEISRLEQQK----QILRERLANLERQLEELEAQLEELESKLDELAEEL-----------AELEEKLE-ELKEELESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 989 MEMAEEERLEYQQQklaaeEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAAL----DKHLHFHQELSKEASGLQ 1064
Cdd:TIGR02168 357 EAELEELEAELEEL-----ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLerleDRRERLQQEIEELLKKLE 431
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
811-1073 |
5.09e-04 |
|
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: 43.68 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 811 VAIDGRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKA-SRDRIRIEKAEMRwLKVEQRRREQEELTWLHKEQLE 889
Cdd:TIGR02794 41 VLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQrAAEQARQKELEQR-AAAEKAAKQAEQAAKQAEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 890 KAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQqeaaeraea 969
Cdd:TIGR02794 120 QAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAK--------- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 970 ekqrqkelemqlAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKqeeeAAKLALEEATKLAQEQIRQKAALDKH 1049
Cdd:TIGR02794 191 ------------AEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERK----ADEAELGDIFGLASGSNAEKQGGARG 254
|
250 260
....*....|....*....|....*.
gi 1720355882 1050 LHFHQELSKEASGLQWT--QNISRPW 1073
Cdd:TIGR02794 255 AAAGSEVDKYAAIIQQAiqQNLYDDP 280
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
928-1048 |
6.69e-04 |
|
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: 41.31 E-value: 6.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 928 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraeAEKQRQKELEMQLAEEQKRLMEMAEEErleyqqqklAAE 1007
Cdd:COG0711 44 ERAKEEAEAALAEYEEKLAEARAEAAEIIAEARK-------EAEAIAEEAKAEAEAEAERIIAQAEAE---------IEQ 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1720355882 1008 EKARQEAEERrkqeEEAAKLALEEATKLAQEQI---RQKAALDK 1048
Cdd:COG0711 108 ERAKALAELR----AEVADLAVAIAEKILGKELdaaAQAALVDR 147
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
799-1048 |
7.57e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 799 QLSLELDALESQ-VAIDGRLSSIQATDVasdmECEEERshEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVE----QR 873
Cdd:TIGR02168 751 QLSKELTELEAEiEELEERLEEAEEELA----EAEAEI--EELEAQIEQLKEELKALREALDELRAELTLLNEEaanlRE 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 874 RREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQ 953
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 954 EIQRKKQQEAAERAeaeKQRQK---------ELEMQLAEEQKRLMEMAEEErLEYQQQKLAAEEKARQEAEERRKQEEEA 1024
Cdd:TIGR02168 905 ELESKRSELRRELE---ELREKlaqlelrleGLEVRIDNLQERLSEEYSLT-LEEAEALENKIEDDEEEARRRLKRLENK 980
|
250 260 270
....*....|....*....|....*....|....
gi 1720355882 1025 AK-------LALEEATKLAQEQI---RQKAALDK 1048
Cdd:TIGR02168 981 IKelgpvnlAAIEEYEELKERYDfltAQKEDLTE 1014
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
840-1064 |
7.85e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 840 PSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQrleee 919
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 920 rqqqeeaekkrRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMqlAEEQKRLMEmAEEERLEY 999
Cdd:COG4942 89 -----------EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRR--LQYLKYLAP-ARREQAEE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720355882 1000 QQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 1064
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
710-1044 |
7.89e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 710 HQAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELTPKKEKLGRKMKRTHKERNMEMAAGLSKSDITNSKEAGGTSHQG 789
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 790 LLRSHSAAGQLSLELDALESQVAIDGRLSSIQATDVASDMECEEE----------RSHEDPSKALQDKKQQEKASRDRIR 859
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaaalqnivvEDDEVAAAAIEYLKAAKAGRATFLP 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 860 IEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARE 939
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 940 RARQQQEELRRKLQEIQRKKQQEAAE--RAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEER 1017
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELaeRLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
330 340
....*....|....*....|....*..
gi 1720355882 1018 RKQEEEAAKLALEEATKLAQEQIRQKA 1044
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEEL 765
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
946-1048 |
8.99e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 8.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 946 EELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMaeEERLEYQQQKLAAEEKARQEAEERRKQEEEaa 1025
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEAL--KARWEAEKELIEEIQELKEELEQRYGKIPE-- 489
|
90 100
....*....|....*....|...
gi 1720355882 1026 klaLEEATKLAQEQIRQKAALDK 1048
Cdd:COG0542 490 ---LEKELAELEEELAELAPLLR 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
933-1061 |
9.28e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 9.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 933 QLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQ------RQKELEMQLAEEQKRLMEmAEEERLEYQQQkLAA 1006
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlarleaEVEQLEERIAQLSKELTE-LEAEIEELEER-LEE 772
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355882 1007 EEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAAL-DKHLHFHQELSKEAS 1061
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtLLNEEAANLRERLES 828
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
928-1043 |
9.35e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 928 KKRRLQLQAARERARQQQEELRRKLQEIQRKkqqeaaeraeaEKQRQKELEMQLAEEQKRLMEMAE-EERLEYQQQKLAA 1006
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRK-----------IGEIEKEIEQLEQEEEKLKERLEElEEDLSSLEQEIEN 755
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1720355882 1007 EEKARQEAEER-RKQEEEAAKLALEEAT---KLAQEQIRQK 1043
Cdd:TIGR02169 756 VKSELKELEARiEELEEDLHKLEEALNDleaRLSHSRIPEI 796
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
928-1029 |
9.75e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 9.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 928 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeAAERAEAEKQRQKELEMQLAEEQKRLMEM-AEEERLEYQQQKLAA 1006
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAA-LEALKAERQKLLARLEKELAELAAELAELqQEAEELEALIARLEA 234
|
90 100
....*....|....*....|...
gi 1720355882 1007 EEKARQEAEERRKQEEEAAKLAL 1029
Cdd:COG4942 235 EAAAAAERTPAAGFAALKGKLPW 257
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
711-1061 |
1.16e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 711 QAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELTPKKEKLGRKMKRTHKE------RNMEMAAGLSKS---DITNSKE 781
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEdknmalRKAEEAKKAEEArieEVMKLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 782 AGGTSHQGLLRSHSAAGQLSLELDALESQVAIDGRLSSIQATDV--ASDMECEEE----RSHEDPSKALQDKKQQEKASR 855
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkkAEELKKAEEenkiKAAEEAKKAEEDKKKAEEAKK 1682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 856 DRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAekmkeelelEQQRRTEENRLRKQRleeerqqqeeaekkrrlQLQ 935
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA---------EELKKAEEENKIKAE-----------------EAK 1736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 936 AARERARQQQEELRRKLQEiQRKKQQEAAERAEAEKQRQKELEMQLAEEQKR---LMEMAEEERLEYQQQKLAAEEKARQ 1012
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEedeKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1720355882 1013 EAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEAS 1061
Cdd:PTZ00121 1816 EGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDG 1864
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
928-1034 |
1.26e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 928 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQR-----QKELEMQ------LAEEQKRLMEMAE--- 993
Cdd:COG1579 44 EARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealQKEIESLkrrisdLEDEILELMERIEele 123
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1720355882 994 ------EERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATK 1034
Cdd:COG1579 124 eelaelEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
935-1045 |
1.31e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.72 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 935 QAARERARQQQEELRRKLQEIQRK-----KQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEK 1009
Cdd:COG3064 11 EAAAQERLEQAEAEKRAAAEAEQKakeeaEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAE 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 1720355882 1010 ARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1045
Cdd:COG3064 91 KKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAK 126
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
938-1045 |
1.31e-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: 39.90 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 938 RERARQQQEELRRKLQEIQRKKQQEAAERaeaekQRQKELEMQLAEEQKRLMEmaEEERLEYQQQKL-----AAEEKARQ 1012
Cdd:pfam20492 1 REEAEREKQELEERLKQYEEETKKAQEEL-----EESEETAEELEEERRQAEE--EAERLEQKRQEAeeekeRLEESAEM 73
|
90 100 110
....*....|....*....|....*....|...
gi 1720355882 1013 EAEERRKQEEEAAklALEEATKLAQEQIRQKAA 1045
Cdd:pfam20492 74 EAEEKEQLEAELA--EAQEEIARLEEEVERKEE 104
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
799-1064 |
1.39e-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: 42.75 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 799 QLSLELDALESQVA-IDGRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQ 877
Cdd:TIGR02169 748 SLEQEIENVKSELKeLEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 878 EELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEK---KRRLQLQAARERARQQQEELRRKLQE 954
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRdleSRLGDLKKERDELEAQLRELERKIEE 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 955 IQRKKQQeaaeraeaEKQRQKELEMQLAEEQKRLMEM-AEEERLEYQQQKLAAEEKARQEaeerrKQEEEAAKLALEEAT 1033
Cdd:TIGR02169 908 LEAQIEK--------KRKRLSELKAKLEALEEELSEIeDPKGEDEEIPEEELSLEDVQAE-----LQRVEEEIRALEPVN 974
|
250 260 270
....*....|....*....|....*....|..
gi 1720355882 1034 KLA-QEQIRQKAALDKHLHFHQELSKEASGLQ 1064
Cdd:TIGR02169 975 MLAiQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
833-1059 |
1.53e-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: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 833 EERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELtwLHKEQLEKAEKMKEELELEQQRRTEENRLR 912
Cdd:TIGR00618 275 QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRS--RAKLLMKRAAHVKQQSSIEEQRRLLQTLHS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 913 KQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMA 992
Cdd:TIGR00618 353 QEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQ 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 993 EEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQ-EQIRQKAALDK--HLHFHQELSKE 1059
Cdd:TIGR00618 433 QELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTkEQIHLQETRKKavVLARLLELQEE 502
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
928-1034 |
1.66e-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: 41.90 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 928 KKRRLQLQAARERARQQQE--------ELRRKLQEiQRKKQqeaaeraeaekQRQKELEMQLAEEQKRLMEMAEEERLEY 999
Cdd:pfam07767 209 KKRLKEEEKLERVLEKIAEsaataearEEKRKTKA-QRNKE-----------KRRKEEEREAKEEKALKKKLAQLERLKE 276
|
90 100 110
....*....|....*....|....*....|....*
gi 1720355882 1000 QQQKLAAEEKARQEAEERRKQEEEAAKLALEEATK 1034
Cdd:pfam07767 277 IAKEIAEKEKEREEKAEARKREKRKKKKEEKKLRP 311
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
847-1043 |
1.71e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 847 KKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEA 926
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 927 EKKRRLQLQAarERARQQQEELRRKLQEIQRKkqqeaaeraeaeKQRQKELEMQLAEEQKRLMEMAEEERLeYQQQKLAA 1006
Cdd:PRK03918 307 DELREIEKRL--SRLEEEINGIEERIKELEEK------------EERLEELKKKLKELEKRLEELEERHEL-YEEAKAKK 371
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720355882 1007 EEKARQEAEERRKQEEEAAKLaLEEATKlAQEQIRQK 1043
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKE-LEELEK-AKEEIEEE 406
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
928-1039 |
2.50e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 928 KKRRLQLQAAR-ERARQQQEELRRKLQEIQRK-KQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKla 1005
Cdd:PRK00409 528 LERELEQKAEEaEALLKEAEKLKEELEEKKEKlQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVK-- 605
|
90 100 110
....*....|....*....|....*....|....
gi 1720355882 1006 aeekaRQEAEERRKQEEEAAKLALEEATKLAQEQ 1039
Cdd:PRK00409 606 -----AHELIEARKRLNKANEKKEKKKKKQKEKQ 634
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
832-1055 |
2.84e-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: 41.65 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 832 EEERSHEDPSKALQDKKQQEKAS-RDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQqrrTEENR 910
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHkRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQ---AELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 911 LRKQRLEEERQQQeeaeKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraEAEKQRQKELEMQLAEEQKRLME 990
Cdd:pfam05557 80 LKKKYLEALNKKL----NEKESQLADAREVISCLKNELSELRRQIQRAELE------LQSTNSELEELQERLDLLKAKAS 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355882 991 MAEE--ERLEYQQQKLAAEEKARQEAEERRKQEEEAAklaleEATKLAQEQIRQKAALDKHLHFHQE 1055
Cdd:pfam05557 150 EAEQlrQNLEKQQSSLAEAEQRIKELEFEIQSQEQDS-----EIVKNSKSELARIPELEKELERLRE 211
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
930-1060 |
2.92e-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: 41.06 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 930 RRLQLQAARERARQQQEELRRKLQEIQRKKQQEAA-----ERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKL 1004
Cdd:pfam13868 43 RRLDEMMEEERERALEEEEEKEEERKEERKRYRQEleeqiEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKL 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355882 1005 AAEEKARQEAEE------RRKQEEeaaKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEA 1060
Cdd:pfam13868 123 EKQRQLREEIDEfneeqaEWKELE---KEEEREEDERILEYLKEKAEREEEREAEREEIEEE 181
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
928-1050 |
3.17e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.29 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 928 KKRRLQLQAARERARQQQEELRRKLQEIQ--------RKKQQEAAERAEAEKQRQKELEMQ------LAEEQKRLMEMAE 993
Cdd:COG1579 41 AALEARLEAAKTELEDLEKEIKRLELEIEevearikkYEEQLGNVRNNKEYEALQKEIESLkrrisdLEDEILELMERIE 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355882 994 EERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLAlEEATKLAQEQIRQKAALDKHL 1050
Cdd:COG1579 121 ELEEELAELEAELAELEAELEEKKAELDEELAELE-AELEELEAEREELAAKIPPEL 176
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
944-1060 |
3.27e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 40.77 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 944 QQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEE 1023
Cdd:PRK06669 31 SIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAKEELLKKTDEASSIIEKLQMQIEREQEEWEE 110
|
90 100 110
....*....|....*....|....*....|....*..
gi 1720355882 1024 AAKLALEEATKLAQEQIRQKaALDKHLHFHQELSKEA 1060
Cdd:PRK06669 111 ELERLIEEAKAEGYEEGYEK-GREEGLEEVRELIEQL 146
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
932-1046 |
3.66e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.64 E-value: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 932 LQLQAARERA-RQQQEELRRKLQEIQRKKQQEAAEraeaeKQRQKELEMQLAEEQKRLMEMaeEERLEYQQQKLaaEEKA 1010
Cdd:cd16269 176 LQSKEAEAEAiLQADQALTEKEKEIEAERAKAEAA-----EQERKLLEEQQRELEQKLEDQ--ERSYEEHLRQL--KEKM 246
|
90 100 110
....*....|....*....|....*....|....*.
gi 1720355882 1011 RQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAAL 1046
Cdd:cd16269 247 EEERENLLKEQERALESKLKEQEALLEEGFKEQAEL 282
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
935-1030 |
3.92e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 40.73 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 935 QAARERARQQQEELRRKLQEIQRKKQQEaaeraeaeKQRQKELEMQLAEEqkrlMEMaEEERLEYQQQKLAAEEKARQEA 1014
Cdd:pfam02841 210 RAKAEAAEAEQELLREKQKEEEQMMEAQ--------ERSYQEHVKQLIEK----MEA-EREQLLAEQERMLEHKLQEQEE 276
|
90
....*....|....*.
gi 1720355882 1015 EERRKQEEEAAKLALE 1030
Cdd:pfam02841 277 LLKEGFKTEAESLQKE 292
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
935-1042 |
4.55e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 935 QAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQ--KELEMQLAEEQKRLmemaeEERLEYQQQKlaAEEKARQ 1012
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELValEGLAAELEEKQQEL-----EAQLEQLQEK--AAETSQE 213
|
90 100 110
....*....|....*....|....*....|...
gi 1720355882 1013 EAEERRKQEEEAAK-LALEEAT--KLAQEQIRQ 1042
Cdd:PRK11448 214 RKQKRKEITDQAAKrLELSEEEtrILIDQQLRK 246
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
971-1047 |
4.81e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 38.19 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 971 KQRQKELEMQLAEEQKRLMEMaeEERLEYQQQKLAaeeKARQEAEERRKQEEEAAKLALEEATKLAQ---EQIRQKAALD 1047
Cdd:cd06503 29 DEREEKIAESLEEAEKAKEEA--EELLAEYEEKLA---EARAEAQEIIEEARKEAEKIKEEILAEAKeeaERILEQAKAE 103
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
948-1045 |
5.00e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 38.45 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 948 LRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLME-MAEEERLEYQQQKLAAE--EKARQEAEERRKQEEEA 1024
Cdd:pfam00430 20 AWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEaRAEAQEIIENAKKRAEKlkEEIVAAAEAEAERIIEQ 99
|
90 100
....*....|....*....|.
gi 1720355882 1025 AKLALEEATKLAQEQIRQKAA 1045
Cdd:pfam00430 100 AAAEIEQEKDRALAELRQQVV 120
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
935-1023 |
5.02e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 40.25 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 935 QAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEM---QLAEEQKRLMEmaeeerLEYQQQKLAAEEKAR 1011
Cdd:cd16269 204 RAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEereNLLKEQERALE------SKLKEQEALLEEGFK 277
|
90
....*....|..
gi 1720355882 1012 QEAEERRKQEEE 1023
Cdd:cd16269 278 EQAELLQEEIRS 289
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
869-1044 |
6.68e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 869 KVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEaekKRRLQLQAARER-------- 940
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE---REIAELEAELERldassddl 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 941 --ARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQkelemQLAEEQKRLMEMAEE-ERLEYQQQKLAAEEKARQEAEER 1017
Cdd:COG4913 688 aaLEEQLEELEAELEELEEELDELKGEIGRLEKELE-----QAEEELDELQDRLEAaEDLARLELRALLEERFAAALGDA 762
|
170 180
....*....|....*....|....*..
gi 1720355882 1018 RkqeEEAAKLALEEATKLAQEQIRQKA 1044
Cdd:COG4913 763 V---ERELRENLEERIDALRARLNRAE 786
|
|
| RIB43A |
pfam05914 |
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar ... |
853-1050 |
7.36e-03 |
|
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar microtubules contain a specialized set of protofilaments, termed ribbons, that are composed of tubulin and several associated proteins. RIB43A was first characterized in the unicellular biflagellate, Chlamydomonas reinhardtii although highly related sequences are present in several higher eukaryotes including humans. The function of this protein is unknown although the structure of RIB43A and its association with the specialized protofilament ribbons and with basal bodies is relevant to the proposed role of ribbons in forming and stabilising doublet and triplet microtubules and in organizing their three-dimensional structure. Human RIB43A homologs could represent a structural requirement in centriole replication in dividing cells.
Pssm-ID: 461780 [Multi-domain] Cd Length: 372 Bit Score: 39.88 E-value: 7.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 853 ASRDRIRIEKAEMR-WLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEerqqqeeaekKRR 931
Cdd:pfam05914 141 NREERKKLQQEQMReWLEQQIEEKKQAEEEEKHAELLYDQKRLERDRRALELAKLEEECRRAVNAAT----------KNF 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 932 LQLQAARERARQQQEELRR---KLQEIQ---------RKKQQEAAER--------------AEAEKQRQKELEMQLAEEQ 985
Cdd:pfam05914 211 NQALAAEQAERRRLEKRQEqedNLAEIYnhltsdlltENPEVAQSSLgphrvipdrwkgmsPEQLKEIRKEQEQQREEKE 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720355882 986 KRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLAlEEATKLAQEQIRQKAALDKHL 1050
Cdd:pfam05914 291 RRREEEKQRDAEWDRQRLELARAALLLEREQQRLRRELRRQLD-EENLQLAQEQKARQEYLNKEV 354
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
851-1064 |
8.39e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 39.63 E-value: 8.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 851 EKASRDRIRIEKAEMRWlkVEQRRREQE-ELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKK 929
Cdd:pfam15558 18 KEEQRMRELQQQAALAW--EELRRRDQKrQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 930 RRLQLQAaRERARQ-------QQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERL-EYQQ 1001
Cdd:pfam15558 96 WREQAED-QENQRQeklerarQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVqENNL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355882 1002 QKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEqIRQKAALDKHLHFHQELSKEASGLQ 1064
Cdd:pfam15558 175 SELLNHQARKVLVDCQAKAEELLRRLSLEQSLQRSQE-NYEQLVEERHRELREKAQKEEEQFQ 236
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
828-1042 |
8.47e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 39.63 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 828 DMECEEERSHEDPSKALQDKK------QQEKASRDRIR--IEKAEMRWLKVEQRRREQEELTWLHKEQ--------LEKA 891
Cdd:pfam15558 75 GREERRRADRREKQVIEKESRwreqaeDQENQRQEKLEraRQEAEQRKQCQEQRLKEKEEELQALREQnslqlqerLEEA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 892 EKMKEELELEQQRR-TEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAE 970
Cdd:pfam15558 155 CHKRQLKEREEQKKvQENNLSELLNHQARKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEERHRELREKAQKEEEQ 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355882 971 KQRQKELEMQLAEEQKRLMEM-AEEERLEYQQQKLAAEEKARQEAEERRKQEEE------AAKLALEEATKLAQEQIRQ 1042
Cdd:pfam15558 235 FQRAKWRAEEKEEERQEHKEAlAELADRKIQQARQVAHKTVQDKAQRARELNLEreknhhILKLKVEKEEKCHREGIKE 313
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
928-1037 |
8.83e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.81 E-value: 8.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 928 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraeaEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAE 1007
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAE--------QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
90 100 110
....*....|....*....|....*....|
gi 1720355882 1008 EKARQEAEERRKQEEEAAKLALEEATKLAQ 1037
Cdd:COG3883 218 AAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
928-1050 |
8.87e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 8.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 928 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAeKQRQKELEmQLAEEQKRLMEMAEEERLEYQQQKLAAE 1007
Cdd:COG4372 69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA-EELQEELE-ELQKERQDLEQQRKQLEAQIAELQSEIA 146
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1720355882 1008 EKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHL 1050
Cdd:COG4372 147 EREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
929-1048 |
9.64e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 39.74 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355882 929 KRRLQlQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEE 1008
Cdd:pfam09731 293 HREID-QLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLRTELE 371
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1720355882 1009 KARQEAEERRKQEEEAAKLALEEA------TKLAQEQIRQKAALDK 1048
Cdd:pfam09731 372 RQAEAHEEHLKDVLVEQEIELQREflqdikEKVEEERAGRLLKLNE 417
|
|
| |
