|
Name |
Accession |
Description |
Interval |
E-value |
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
580-1090 |
3.18e-159 |
|
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: 483.30 E-value: 3.18e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 580 SSRLAQAAESQGAPQSLEAAAQKTGEPQRCINKGLICSNEKEFYTRKLHIDMTPFLKERGSELDSHEEPGGPLRGNAKDS 659
Cdd:pfam15709 3 TSPLTQTTEEQGAQQSLEAAAQKTGEPQSCINKGLICSNRKEFYTRKLHIDMTPFLKDSGEALDSHEEPGEPLGENHQDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 660 QDPELRNKTLACLSTSLAEYNQPSEADTLKSMDG-DYNVHHLHRGPLKREPAFPKKLA----SETPRKKKKRRS-KLLNQ 733
Cdd:pfam15709 83 QDPEPRSVTLSPLSASLGEHIQTPEADTVQNGDGeDYDVHHLHRGLPRHRPESPEKLTavdtSLLPRAREGKTEpRLFNQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 734 KTGVGINHG-KDLVDKAKRKKRTKTHQAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELTPKKEKLGRKMKRTHKERN 812
Cdd:pfam15709 163 ETPASISHAeRELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 813 MEMAAGLSKSDITNSKEAGGTSHQGLLRSHSAAGQ--LSLELDALESQVAIDGRLSSIQATDVASDMECEEERSHEDPSK 890
Cdd:pfam15709 243 LEVAAELSGPDVINSKETEDASERGAFSSDSVVEDpwLSSKYDAEESQVSIDGRSSPTQTFVVTGNMESEEERSEEDPSK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 891 ALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQ 970
Cdd:pfam15709 323 ALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 971 QEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQ 1050
Cdd:pfam15709 403 QEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQ 482
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1720355871 1051 KLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQ 1090
Cdd:pfam15709 483 KQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
847-1109 |
1.47e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 847 QLSLELDALESQVA-IDGRLSSIQATDVASDMECEEER-SHEDPSKALQDKKQQE-KASRDRIRIEKAEMRwlKVEQRRR 923
Cdd:COG1196 236 ELEAELEELEAELEeLEAELEELEAELAELEAELEELRlELEELELELEEAQAEEyELLAELARLEQDIAR--LEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 924 EQEELtwlhkEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEI 1003
Cdd:COG1196 314 LEERL-----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1004 QRKKQQeaaerAEAEKQRQKELEMQLAEEQKRLmEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKL 1083
Cdd:COG1196 389 LEALRA-----AAELAAQLEELEEAEEALLERL-ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260
....*....|....*....|....*.
gi 1720355871 1084 AQEQIRQKAALDKHLHFHQELSKEAS 1109
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAE 488
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
880-1096 |
3.16e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 74.79 E-value: 3.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 880 EEERSHEDPSKAlQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELtwLHKEQLEKAEKMKEELELEQQRRTEENRl 959
Cdd:PTZ00121 1572 AEEDKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK--IKAEELKKAEEEKKKVEQLKKKEAEEKK- 1647
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 960 rkqrLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRklQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEM 1039
Cdd:PTZ00121 1648 ----KAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK--AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720355871 1040 --AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLA--LEEATKLAQEQIRQKAALDK 1096
Cdd:PTZ00121 1722 kkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAhlKKEEEKKAEEIRKEKEAVIE 1782
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
895-1112 |
6.09e-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: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 895 KKQQEKASR-----DRIRIEKAEMRWLKVEQRRREQEELtwlhKEQLEKAEKMKEELEleQQRRTEENRLRKqrleeerq 969
Cdd:COG1196 206 ERQAEKAERyrelkEELKELEAELLLLKLRELEAELEEL----EAELEELEAELEELE--AELAELEAELEE-------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 970 qqeeaekkRRLQLQAARERARQQQEELRRKLQEIQR--KKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEE----- 1042
Cdd:COG1196 272 --------LRLELEELELELEEAQAEEYELLAELARleQDIARLEERRRELEERLEELEEELAELEEELEELEEEleele 343
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1043 ERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 1112
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
869-1096 |
1.84e-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: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 869 QATDVASDMECEEERSHEDPSKALQDKKQQ-EKASRDRIRIEKAEMRWLKVEQRRREQEELTWlhKEQLEKAEKMKEELE 947
Cdd:pfam17380 332 QAAIYAEQERMAMERERELERIRQEERKRElERIRQEEIAMEISRMRELERLQMERQQKNERV--RQELEAARKVKILEE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 948 LEQqrRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKlQEIQRKKQQEAAERAEAEKQRQKELEM 1027
Cdd:pfam17380 410 ERQ--RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQ-QQVERLRQQEEERKRKKLELEKEKRDR 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1028 QLAEEQKRLM----------EMAEEER--------LEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIR 1089
Cdd:pfam17380 487 KRAEEQRRKIlekeleerkqAMIEEERkrkllekeMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERS 566
|
....*..
gi 1720355871 1090 QKAALDK 1096
Cdd:pfam17380 567 RLEAMER 573
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
980-1093 |
2.06e-12 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 70.22 E-value: 2.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 980 LQLQAARERARQQQEElRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKAR 1059
Cdd:PRK09510 92 LQQKQAAEQERLKQLE-KERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKK 170
|
90 100 110
....*....|....*....|....*....|....
gi 1720355871 1060 QEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1093
Cdd:PRK09510 171 AEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAE 204
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
891-1112 |
5.37e-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: 5.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 891 ALQDKKQQEKASRDRIRIEKAEmrwlkvEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQ 970
Cdd:COG1196 231 LLKLRELEAELEELEAELEELE------AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 971 QEEaeKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAeKQRQKELEMQLAEEQKRLMEMAEE--ERLEYQ 1048
Cdd:COG1196 305 ARL--EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA-EEELEEAEAELAEAEEALLEAEAElaEAEEEL 381
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355871 1049 QQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 1112
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
847-1102 |
8.21e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 8.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 847 QLSLELDALESQVAiDGRLSSIQATDVASDMECEEERSHEDPSKALQDKK-QQEKASRDRIRIEKAEMRWLKVEQRRREQ 925
Cdd:COG1196 257 ELEAELAELEAELE-ELRLELEELELELEEAQAEEYELLAELARLEQDIArLEERRRELEERLEELEEELAELEEELEEL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 926 EELTwlhKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERA--RQQQEELRRKLQEI 1003
Cdd:COG1196 336 EEEL---EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAelAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1004 QRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLmemAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKL 1083
Cdd:COG1196 413 LERLERLEEELEELEEALAELEEEEEEEEEALE---EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
250
....*....|....*....
gi 1720355871 1084 AQEQIRQKAALDKHLHFHQ 1102
Cdd:COG1196 490 AARLLLLLEAEADYEGFLE 508
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
880-1112 |
2.23e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.63 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 880 EEERSHEDPSKALQDKKQQEKASRDRIR----IEKAEMRwLKVEQRRREQEELTWLHKE-----QLEKAEKMKEELELEQ 950
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKkaeeLKKAEEK-KKAEEAKKAEEDKNMALRKaeeakKAEEARIEEVMKLYEE 1603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 951 QRRTEENRLRKQRLEEERQQQ---EEAEKKRRLQLQAARERARQQQEELRRKLQEIQ------RKKQQEAAERAEAEKQR 1021
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAKIKAEElkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKikaaeeAKKAEEDKKKAEEAKKA 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1022 QKElEMQLAEEQKRlmeMAEEERLEYQQQKLAAEEKARQE----AEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKH 1097
Cdd:PTZ00121 1684 EED-EKKAAEALKK---EAEEAKKAEELKKKEAEEKKKAEelkkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
|
250
....*....|....*
gi 1720355871 1098 LHFHQELSKEASGLQ 1112
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIR 1774
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
984-1108 |
2.37e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 67.14 E-value: 2.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 984 AARERARQQQEELRRKLQEIQRKKQQeaaeraeaeKQRQKELEMQLAEEQKRLMEMaEEERLEYQQQKLAAEEKARQEAE 1063
Cdd:PRK09510 60 VVEQYNRQQQQQKSAKRAEEQRKKKE---------QQQAEELQQKQAAEQERLKQL-EKERLAAQEQKKQAEEAAKQAAL 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355871 1064 ERRKQEEEAAKLA-------------LEEATKLAQEQIRQKAALDKHLHFHQELSKEA 1108
Cdd:PRK09510 130 KQKQAEEAAAKAAaaakakaeaeakrAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKA 187
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
890-1112 |
2.56e-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: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 890 KALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEE-NRLRKqrleeer 968
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELElEEAQA------- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 969 qqQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQR-QKELEMQLAEEQKRLMEMAEEERLEY 1047
Cdd:COG1196 289 --EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELeELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720355871 1048 QQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQ 1112
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
976-1096 |
1.01e-10 |
|
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: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 976 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEyQQQKLAAE 1055
Cdd:TIGR02794 53 NRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE-AKAKQAAE 131
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1720355871 1056 EKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDK 1096
Cdd:TIGR02794 132 AKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAK 172
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
890-1081 |
2.40e-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: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 890 KALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEqleKAEKMKEELELEQQRRTEENRLRKQRLEEERQ 969
Cdd:pfam17380 399 EAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEE---RAREMERVRLEEQERQQQVERLRQQEEERKRK 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 970 QQEEAEKKRRLQLQAARERA--RQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEY 1047
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKilEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQ 555
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720355871 1048 QQQKLAAEEKARQEAEERRKQ------EEEAAKLALEEAT 1081
Cdd:pfam17380 556 EQMRKATEERSRLEAMEREREmmrqivESEKARAEYEATT 595
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
880-1096 |
8.01e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 880 EEERSHEDPSKAlQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQL----EKAEKMKEELELEQQRRTE 955
Cdd:PTZ00121 1215 EEARKAEDAKKA-EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaikaEEARKADELKKAEEKKKAD 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 956 ENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQE------IQRKKQQEAAERAEAEKQRQKELEMQL 1029
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEakkaaeAAKAEAEAAADEAEAAEEKAEAAEKKK 1373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1030 AEEQKR---LMEMAEEERLEYQQQKLAAEEKarQEAEERRKQEEEAAKlaLEEATKLAQEQIRQKAALDK 1096
Cdd:PTZ00121 1374 EEAKKKadaAKKKAEEKKKADEAKKKAEEDK--KKADELKKAAAAKKK--ADEAKKKAEEKKKADEAKKK 1439
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
880-1092 |
8.43e-10 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.62 E-value: 8.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 880 EEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENR- 958
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKk 1553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 959 ---LRKQRLEEERQQQEEAEKKRRLQLQAARE--RARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMqlAEEQ 1033
Cdd:PTZ00121 1554 aeeLKKAEEKKKAEEAKKAEEDKNMALRKAEEakKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK--AEEE 1631
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1034 KRLMEM-----------AEEERLEYQQQKLAAEEKARQEAEERRKQEEeaAKLAlEEATKLAQEQIRQKA 1092
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 ... |
983-1108 |
1.00e-08 |
|
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: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 983 QAARERARQQQEELRRKLQEIQRKKQQeaaeraeaeKQRQKELEMQLAEEQKRLMEM-----AEEERLEYQQQKLAAEEK 1057
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKL---------EQQAEEAEKQRAAEQARQKELeqraaAEKAAKQAEQAAKQAEEK 117
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1720355871 1058 ARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEA 1108
Cdd:TIGR02794 118 QKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKA 168
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
877-1096 |
1.72e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 877 MECEEERSHEDPSKALQDKKQQEKASRDRIRiekaemrwlKVEQRRREQEELTwlHKEQLEKAEKMKEELELEQQRRTEE 956
Cdd:PTZ00121 1272 IKAEEARKADELKKAEEKKKADEAKKAEEKK---------KADEAKKKAEEAK--KADEAKKKAEEAKKKADAAKKKAEE 1340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 957 NRLRKQRLEEERQQQEEAEKKRRLQLQAAR---ERARQQQEELRRKLQEIqrKKQQEAAERAEAEKQRQKELEMQLAEEQ 1033
Cdd:PTZ00121 1341 AKKAAEAAKAEAEAAADEAEAAEEKAEAAEkkkEEAKKKADAAKKKAEEK--KKADEAKKKAEEDKKKADELKKAAAAKK 1418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355871 1034 K--RLMEMAEEERLEYQQQKLAAE----EKARQEAEERRKQEE-----EAAKLAlEEATKLAQEQIRQKAALDK 1096
Cdd:PTZ00121 1419 KadEAKKKAEEKKKADEAKKKAEEakkaDEAKKKAEEAKKAEEakkkaEEAKKA-DEAKKKAEEAKKADEAKKK 1491
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
890-1090 |
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: 58.60 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 890 KALQDKKQQEKASR---DRIRIEKAEmRWLKVEQRRR--------------------EQEELTWLHKEQLEKAEKMKEEL 946
Cdd:pfam17380 282 KAVSERQQQEKFEKmeqERLRQEKEE-KAREVERRRKleeaekarqaemdrqaaiyaEQERMAMERERELERIRQEERKR 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 947 ELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRL--QLQAAReRARQQQEELRRKLQEIQRKKQQeaaERAEAEKQRQKE 1024
Cdd:pfam17380 361 ELERIRQEEIAMEISRMRELERLQMERQQKNERVrqELEAAR-KVKILEEERQRKIQQQKVEMEQ---IRAEQEEARQRE 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355871 1025 LEmQLAEEQKRLMEMAEEERLEYQQQKlaaeEKARQEAEERRKQEEEAAKlaLEEATKLAQEQIRQ 1090
Cdd:pfam17380 437 VR-RLEEERAREMERVRLEEQERQQQV----ERLRQQEEERKRKKLELEK--EKRDRKRAEEQRRK 495
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
848-1126 |
2.25e-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: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 848 LSLELDALESQ-VAIDGRLSSIQA--TDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQR--R 922
Cdd:TIGR02169 228 LLKEKEALERQkEAIERQLASLEEelEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAslE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 923 REQEELtwlhKEQLEKAEKmkeeleleQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQE 1002
Cdd:TIGR02169 308 RSIAEK----ERELEDAEE--------RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1003 IQRKKQqeaaERAEAEKQRQKELEM------QLAEEQKRLMEMAE---------EERLEYQQQKLAAEEKARQEAEERRK 1067
Cdd:TIGR02169 376 VDKEFA----ETRDELKDYREKLEKlkreinELKRELDRLQEELQrlseeladlNAAIAGIEAKINELEEEKEDKALEIK 451
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355871 1068 QEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEASGLQWTQNISRPWVYSYF 1126
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
759-1106 |
3.80e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 759 QAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELTPKKEKLGRKMKRTHKERNMEMAAGLSKSDITNSKEAGGTSHQGL 838
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 839 LRSHSAAGQLSLELDALESQVAIDGRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKV 918
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 919 EQRRREQEELTwlhKEQLEKAEKMKEELELEQQRRTEENRLR---KQRLEEERQQQEEAEKKRRLQLQAARERarqQQEE 995
Cdd:PTZ00121 1401 EEDKKKADELK---KAAAAKKKADEAKKKAEEKKKADEAKKKaeeAKKADEAKKKAEEAKKAEEAKKKAEEAK---KADE 1474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 996 LRRKLQEIQRK---KQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKarQEAEERRKQEE-- 1070
Cdd:PTZ00121 1475 AKKKAEEAKKAdeaKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA--KKAEEKKKADElk 1552
|
330 340 350
....*....|....*....|....*....|....*.
gi 1720355871 1071 EAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSK 1106
Cdd:PTZ00121 1553 KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
830-1087 |
7.32e-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: 7.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 830 AGGTSHQGLLRSHSAAGQLSLELDALESQVAI---DGRLSSIQATDVasdmeceeERSHEDPSKALQDKKQQEKASRDRI 906
Cdd:TIGR02168 657 PGGVITGGSAKTNSSILERRREIEELEEKIEEleeKIAELEKALAEL--------RKELEELEEELEQLRKELEELSRQI 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 907 RIEKAEMRWLKVEQRRREQEeltwlhKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAAR 986
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEER------IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 987 ERARQQQEELRRKLQEIQRK--KQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEerLEYQQQKLAAEEKARQEAEE 1064
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAE--IEELEELIEELESELEALLN 880
|
250 260
....*....|....*....|...
gi 1720355871 1065 RRKQEEEAAKLALEEATKLAQEQ 1087
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEEL 903
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
983-1093 |
1.28e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 55.26 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 983 QAARERARQQQEELRRklQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLmEMAEEERLEyQQQKLAAEEKARQEA 1062
Cdd:COG2268 241 EAEAELAKKKAEERRE--AETARAEAEAAYEIAEANAEREVQRQLEIAEREREI-ELQEKEAER-EEAELEADVRKPAEA 316
|
90 100 110
....*....|....*....|....*....|..
gi 1720355871 1063 EERRKQEEEAAKLALEEATKLAQ-EQIRQKAA 1093
Cdd:COG2268 317 EKQAAEAEAEAEAEAIRAKGLAEaEGKRALAE 348
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
886-1096 |
1.81e-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: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 886 EDPSKAL--QDKKQQEKASRDRiRIEKAEMRW---LKVEQRRREQEEltwlhkEQLEKAEKMKEELELEQQRRTEEnrlr 960
Cdd:COG2268 180 EDENNYLdaLGRRKIAEIIRDA-RIAEAEAEReteIAIAQANREAEE------AELEQEREIETARIAEAEAELAK---- 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 961 kqrleeerqqqeeaeKKRRLQLQAARERARQQQE-ELRR--KLQEIQRKKQQEaaeraeaekQRQKELEMQLAEEQKRLM 1037
Cdd:COG2268 249 ---------------KKAEERREAETARAEAEAAyEIAEanAEREVQRQLEIA---------EREREIELQEKEAEREEA 304
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720355871 1038 EMAEEERLEYQQQKLAAEEKARQEAE-ERRKQEEEA-AKLALEEATKLAQEQIRQKAALDK 1096
Cdd:COG2268 305 ELEADVRKPAEAEKQAAEAEAEAEAEaIRAKGLAEAeGKRALAEAWNKLGDAAILLMLIEK 365
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
882-1093 |
3.85e-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: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 882 ERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRK 961
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 962 qrleeerqqqeeaekkRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEM------QLAEEQKR 1035
Cdd:pfam13868 188 ----------------RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELqqareeQIELKERR 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355871 1036 LMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLAlEEATKLAQEQIRQKAA 1093
Cdd:pfam13868 252 LAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHR-RELEKQIEEREEQRAA 308
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
953-1108 |
5.53e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 953 RTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQ-EAAERAEAEKQRQKELEMQLAE 1031
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355871 1032 EQKRLMEMaeEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEA 1108
Cdd:COG4717 144 LPERLEEL--EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
893-1093 |
1.30e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.56 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 893 QDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQE 972
Cdd:pfam02029 143 NKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVT 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 973 EAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRlmemAEEERleyqqqkl 1052
Cdd:pfam02029 223 TKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKK----REERR-------- 290
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1720355871 1053 aaeeKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1093
Cdd:pfam02029 291 ----KLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERRRA 327
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
987-1076 |
1.37e-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: 49.27 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 987 ERARQQQEELRRKLQEiQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEY-QQQKLAAEEKARQEAE-- 1063
Cdd:pfam05672 39 EEERLRKEELRRRAEE-ERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERlQKQKEEAEAKAREEAErq 117
|
90
....*....|....*..
gi 1720355871 1064 ----ERRKQEEEAAKLA 1076
Cdd:pfam05672 118 rqerEKIMQQEEQERLE 134
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
867-1079 |
1.97e-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: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 867 SIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEmrwlkveQRRREQEELTwlhkEQLEKAEKMKEEL 946
Cdd:pfam13868 135 FNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEE-------EKEREIARLR----AQQEKAQDEKAER 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 947 ELEQQRRTEENRLRKQRLEEERQQQeeaeKKRRLQLQAARERARQQQEELRRKLQEIQR---------KKQQEAAERAEA 1017
Cdd:pfam13868 204 DELRAKLYQEEQERKERQKEREEAE----KKARQRQELQQAREEQIELKERRLAEEAEReeeefermlRKQAEDEEIEQE 279
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355871 1018 EKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEE 1079
Cdd:pfam13868 280 EAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
892-1107 |
1.97e-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: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 892 LQDKKQQEKASRDRIRIEKAEMRwlkvEQRRREQEELtwLHKEQLEKAEKMKEELELEQQRrtEENRLRKQRLEEERQQQ 971
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMME----EERERALEEE--EEKEEERKEERKRYRQELEEQI--EEREQKRQEEYEEKLQE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 972 EEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAE-----EQKRLMEMAEEERLE 1046
Cdd:pfam13868 100 REQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEylkekAEREEEREAEREEIE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720355871 1047 YQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKE 1107
Cdd:pfam13868 180 EEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQA 240
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
836-1086 |
2.29e-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: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 836 QGLLRSHSAAGQLSLELDALESQVAidgRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRdRIRIEKAEMRW 915
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELA---ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA-LLEAEAELAEA 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 916 LKVEQRRREQEEltwlhkeQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEE 995
Cdd:COG1196 378 EEELEELAEELL-------EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 996 LRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKL 1075
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
|
250
....*....|.
gi 1720355871 1076 ALEEATKLAQE 1086
Cdd:COG1196 531 GVEAAYEAALE 541
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
890-1086 |
2.66e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 890 KALQDKKQQEKASRDRIrIEKAEMrwlKVEQRRRE-----QEELTWLhKEQLEKAEKMKEELELEQQRRTE--ENRLRKQ 962
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRI-LEEAKK---EAEAIKKEalleaKEEIHKL-RNEFEKELRERRNELQKLEKRLLqkEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 963 RLEEerqqqeeaeKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraeaekqRQKELE--MQLAEEQ--KRLME 1038
Cdd:PRK12704 102 LELL---------EKREEELEKKEKELEQKQQELEKKEEELEELIEE-----------QLQELEriSGLTAEEakEILLE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720355871 1039 MAEEErleyqqqklaaeekARQEAEERRKQEEEAAKlalEEATKLAQE 1086
Cdd:PRK12704 162 KVEEE--------------ARHEAAVLIKEIEEEAK---EEADKKAKE 192
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
880-1077 |
3.08e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 880 EEERSHEDPSKALQDKKQQEKASRDRIRIEKAEmrwLKVEQRRREQEELTWLHKEQLEKAEkmkeeleleQQRRTEENRL 959
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEE---LREELEKLEKLLQLLPLYQELEALE---------AELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 960 RKQRLEEerqqqeeaekKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEm 1039
Cdd:COG4717 149 EELEERL----------EELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE- 217
|
170 180 190
....*....|....*....|....*....|....*...
gi 1720355871 1040 aEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLAL 1077
Cdd:COG4717 218 -AQEELEELEEELEQLENELEAAALEERLKEARLLLLI 254
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
895-1112 |
3.25e-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: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 895 KKQQEKASRDR-IRIEKAEMRW----LKVEQRRREQEELtwlhKEQLEKAEKMKEELELEQQRRTEE-NRLRKQrleeer 968
Cdd:TIGR02168 206 ERQAEKAERYKeLKAELRELELallvLRLEELREELEEL----QEELKEAEEELEELTAELQELEEKlEELRLE------ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 969 qqqEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraeaEKQRQKELEMQLAEEQKRLMEMAEE-ERLEY 1047
Cdd:TIGR02168 276 ---VSELEEEIEELQKELYALANEISRLEQQKQILRERLAN--------LERQLEELEAQLEELESKLDELAEElAELEE 344
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355871 1048 QQQKLAAE--------EKARQEAEERRKQEEEAAKLALEEATKLAQEQiRQKAALDKHLhfhQELSKEASGLQ 1112
Cdd:TIGR02168 345 KLEELKEElesleaelEELEAELEELESRLEELEEQLETLRSKVAQLE-LQIASLNNEI---ERLEARLERLE 413
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
976-1107 |
3.27e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.93 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 976 KKRRLQLQAARERARQQQE-ELRRKLQEIQRKKQQEaaeraeaeKQRQKELEMQLAEEQKRlmemaeEERLEYQQQKLAA 1054
Cdd:PRK12704 56 KEALLEAKEEIHKLRNEFEkELRERRNELQKLEKRL--------LQKEENLDRKLELLEKR------EEELEKKEKELEQ 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355871 1055 E----EKARQEAEERRKQE----EEAAKLALEEATKLAQEQIRQKAALDKHLHFHQ--ELSKE 1107
Cdd:PRK12704 122 KqqelEKKEEELEELIEEQlqelERISGLTAEEAKEILLEKVEEEARHEAAVLIKEieEEAKE 184
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
847-1084 |
3.36e-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: 3.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 847 QLSLELDALESQVAI-DGRLSSIQATDVASDMECEEERSHEDPSKA----LQDKKQQEKASRDRIRIEKAEMRWLKVEQR 921
Cdd:TIGR02168 292 ALANEISRLEQQKQIlRERLANLERQLEELEAQLEELESKLDELAEelaeLEEKLEELKEELESLEAELEELEAELEELE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 922 RREQEEltwlhKEQLEKAEKMKEELEleQQRRTEENRLRkqrleeerqqqeeAEKKRRLQLQAARERARQQQEELRRKLQ 1001
Cdd:TIGR02168 372 SRLEEL-----EEQLETLRSKVAQLE--LQIASLNNEIE-------------RLEARLERLEDRRERLQQEIEELLKKLE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1002 EIQRKKQQEA----AERAEAEKQRQKELEMQLAEEQKRLMEMAEEER-LEYQQQKLAAEEKARQEAEERRKQEEEAAKLA 1076
Cdd:TIGR02168 432 EAELKELQAEleelEEELEELQEELERLEEALEELREELEEAEQALDaAERELAQLQARLDSLERLQENLEGFSEGVKAL 511
|
....*...
gi 1720355871 1077 LEEATKLA 1084
Cdd:TIGR02168 512 LKNQSGLS 519
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
878-1063 |
3.41e-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: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 878 ECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKaekmkeeLELEQQRRTEEN 957
Cdd:pfam17380 421 EMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEK-------EKRDRKRAEEQR 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 958 R-LRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraEAEKQRQKELEMQLAEEQKRL 1036
Cdd:pfam17380 494 RkILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQ------EMEERRRIQEQMRKATEERSR 567
|
170 180
....*....|....*....|....*..
gi 1720355871 1037 MEMAEEERLEYQQqkLAAEEKARQEAE 1063
Cdd:pfam17380 568 LEAMEREREMMRQ--IVESEKARAEYE 592
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
890-1100 |
3.78e-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: 50.53 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 890 KALQDKKQQEKASRDRIR--IEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEE--NRLRKQRLE 965
Cdd:COG4942 37 AELEKELAALKKEEKALLkqLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEElaELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 966 EERQQQE-------EAEKKRRLQLQAARERARQQQ-EELRRKLQEIQRKKQQeaaerAEAEKQRQKELEMQLAEEQKRLm 1037
Cdd:COG4942 117 GRQPPLAlllspedFLDAVRRLQYLKYLAPARREQaEELRADLAELAALRAE-----LEAERAELEALLAELEEERAAL- 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355871 1038 emaeeERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHF 1100
Cdd:COG4942 191 -----EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
890-1094 |
3.84e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 890 KALQDKKQQ-EKASRDRIRIEKAEMRWL--KVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEE 966
Cdd:COG4717 49 ERLEKEADElFKPQGRKPELNLKELKELeeELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 967 ERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaerAEAEKQRQKELEMQLAEEQKRLMEMAEEERLE 1046
Cdd:COG4717 129 PLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE-----LAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720355871 1047 YQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAAL 1094
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL 251
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
919-1096 |
4.08e-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: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 919 EQRRREQEELtwlhkEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRR 998
Cdd:TIGR02794 61 PAAKKEQERQ-----KKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 999 KLQEIQRKKQQEAaeraeaEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEaEERRKQEEEAAKLALE 1078
Cdd:TIGR02794 136 AEAEAERKAKEEA------AKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAE-EAKAKAEAAKAKAAAE 208
|
170
....*....|....*...
gi 1720355871 1079 EATKLAQEQIRQKAALDK 1096
Cdd:TIGR02794 209 AAAKAEAEAAAAAAAEAE 226
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
880-1089 |
8.52e-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: 8.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 880 EEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEEltwlHKEQLE-KAEKMKEELELEQQRRTEENR 958
Cdd:TIGR02169 204 RREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE----ELEKLTeEISELEKRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 959 lrkqRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeAAERAEAEKQRQKELEMQLAEEQKRLME 1038
Cdd:TIGR02169 280 ----KIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK-LEAEIDKLLAEIEELEREIEEERKRRDK 354
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355871 1039 MAEE-----ERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIR 1089
Cdd:TIGR02169 355 LTEEyaelkEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDR 410
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
981-1093 |
8.64e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 8.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 981 QLQAARERARQQQEELRRKLQEIQRKKQQEaaeraeaeKQRQKELEMQLAEEQKRLMEMAEEERlEYQQQKlAAEEKARQ 1060
Cdd:COG3883 137 ELKADKAELEAKKAELEAKLAELEALKAEL--------EAAKAELEAQQAEQEALLAQLSAEEA-AAEAQL-AELEAELA 206
|
90 100 110
....*....|....*....|....*....|...
gi 1720355871 1061 EAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1093
Cdd:COG3883 207 AAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
887-1096 |
1.14e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 887 DPSKALQD--KKQQEKASRDRirieKAEMRWLKVEQRRREQEEltwlhkEQLEkaekmkeeleleQQRRTEENRLRKQRL 964
Cdd:PRK09510 56 DPGAVVEQynRQQQQQKSAKR----AEEQRKKKEQQQAEELQQ------KQAA------------EQERLKQLEKERLAA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 965 EEERQQQEEAEKKRRLQLQAARERARQQQEElrrklqeiqrkkqqeaaeraeaEKQRQKELEMQLAEEQKRLMEMAEEER 1044
Cdd:PRK09510 114 QEQKKQAEEAAKQAALKQKQAEEAAAKAAAA----------------------AKAKAEAEAKRAAAAAKKAAAEAKKKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1720355871 1045 LEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDK 1096
Cdd:PRK09510 172 EAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEA 223
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
976-1103 |
1.68e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 48.94 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 976 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAE-----EERLEYQQQ 1050
Cdd:PRK12705 33 KEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEkldnlENQLEEREK 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355871 1051 KLAAEEKARQEAEERRKQE-EEAAKLALEEATKL--------AQEQIRQKAALDKH-LHFHQE 1103
Cdd:PRK12705 113 ALSARELELEELEKQLDNElYRVAGLTPEQARKLllklldaeLEEEKAQRVKKIEEeADLEAE 175
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
897-1107 |
2.07e-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: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 897 QQEKASRDRIRIEKAEmrwlKVEQRRREQEeltwlhKEQLEKaekmkeelelEQQRRTEENRLRKQRLEEERQQQEEAEK 976
Cdd:pfam17380 279 QHQKAVSERQQQEKFE----KMEQERLRQE------KEEKAR----------EVERRRKLEEAEKARQAEMDRQAAIYAE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 977 KRRLQLQAARERARQQQEELRRKLQEI----------------------QRKKQQEAAERAEAEKQRQKELEMQ-LAEEQ 1033
Cdd:pfam17380 339 QERMAMERERELERIRQEERKRELERIrqeeiameisrmrelerlqmerQQKNERVRQELEAARKVKILEEERQrKIQQQ 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355871 1034 KRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKE 1107
Cdd:pfam17380 419 KVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQ 492
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
919-1096 |
2.19e-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: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 919 EQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQL--QAARERARQQQEEL 996
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLdyLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 997 RRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLA 1076
Cdd:pfam02463 246 LRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180
....*....|....*....|
gi 1720355871 1077 LEEATKLAQEQIRQKAALDK 1096
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELK 345
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
950-1098 |
2.98e-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: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 950 QQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKqrqkelemQL 1029
Cdd:pfam05262 204 KERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDK--------QV 275
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355871 1030 AEEQKRLMEMAEEE----RLEYQQQKLAAEEKARQEA---EERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHL 1098
Cdd:pfam05262 276 AENQKREIEKAQIEikknDEEALKAKDHKAFDLKQESkasEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSL 351
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
901-1097 |
3.15e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 47.61 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 901 ASRDRIRIEKAEMRWLKVEQRRREQEELtwlhKEQLEKAekmkeeleleQQRRTEENRLRKQRLEEERQQQEEAEKKRRL 980
Cdd:pfam13868 22 KERDAQIAEKKRIKAEEKEEERRLDEMM----EEERERA----------LEEEEEKEEERKEERKRYRQELEEQIEEREQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 981 QLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQ 1060
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAER 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1720355871 1061 EAEERRKQEEE-----------AAKLALEEATKLAQEQIRQKAALDKH 1097
Cdd:pfam13868 168 EEEREAEREEIeeekereiarlRAQQEKAQDEKAERDELRAKLYQEEQ 215
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
987-1090 |
5.29e-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: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 987 ERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERR 1066
Cdd:pfam05672 10 EEAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEERE 89
|
90 100 110
....*....|....*....|....*....|....*
gi 1720355871 1067 -----------KQEEEAAKLALEEATKLAQEQIRQ 1090
Cdd:pfam05672 90 qreqeeqerlqKQKEEAEAKAREEAERQRQEREKI 124
|
|
| DDRGK |
pfam09756 |
DDRGK domain; This is a family of proteins of approximately 300 residues, found in plants and ... |
998-1072 |
6.72e-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: 6.72e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355871 998 RKLQEIQRKKQQEAAEraeaeKQRQKELEMQLAEEQKRLMEMAEEERLEYQ-QQKLAAEEKARQEA---EERRKQEEEA 1072
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 ... |
865-1107 |
6.79e-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: 6.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 865 LSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKV-EQRRREQEELTWLHKEQLEKAEKMK 943
Cdd:pfam02463 254 ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERrKVDDEEKLKESEKEKKKAEKELKKE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 944 EELELEQQRRTEENRLRKQRLEEERQQqeeaekkrrlqlqaarerARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQK 1023
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAEEEEEEE------------------LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1024 ELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEaAKLALEEATKLAQEQIRQKAALDKHLHFHQE 1103
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ-GKLTEEKEELEKQELKLLKDELELKKSEDLL 474
|
....
gi 1720355871 1104 LSKE 1107
Cdd:pfam02463 475 KETQ 478
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
835-1116 |
7.39e-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: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 835 HQGLLRSHSAAGQLSLELDALESQV-AIDGRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQekasrdRIRIEKAEM 913
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELqELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ------QKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 914 RWLKVEQRRREqeeltwlhkEQLEKAEkmkeELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQ 993
Cdd:TIGR02168 312 ANLERQLEELE---------AQLEELE----SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 994 EELRRKLQEIQRKKQQEAAERAeaekqRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAA 1073
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNN-----EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQ 453
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1720355871 1074 K--LALEEATKLAQEQIRQK-AALDKHLHFHQELSKEASGLQWTQN 1116
Cdd:TIGR02168 454 EelERLEEALEELREELEEAeQALDAAERELAQLQARLDSLERLQE 499
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
759-1093 |
8.71e-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: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 759 QAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELtpkKEKLGRKMKRTHKERNMEMAAGLSKSDITNSKEAGGTshQGL 838
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAEL---LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL--RGL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 839 LRSHSAAGQLSLELDALEsQVAIDGRLSSIQATDVASDMECEEERSHEDPSKA----LQDKKQQEKASRDRIRIEKAEMR 914
Cdd:COG1196 523 AGAVAVLIGVEAAYEAAL-EAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflpLDKIRARAALAAALARGAIGAAV 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 915 WLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLR-KQRLEEERQQQEEAEKKRRLQLQAARERARQQQ 993
Cdd:COG1196 602 DLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLReVTLEGEGGSAGGSLTGGSRRELLAALLEAEAEL 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 994 EELRRKLQEIQRKKQQeaaeraeaeKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAA 1073
Cdd:COG1196 682 EELAERLAEEELELEE---------ALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEA 752
|
330 340
....*....|....*....|
gi 1720355871 1074 KLALEEATKLAQEQIRQKAA 1093
Cdd:COG1196 753 LEELPEPPDLEELERELERL 772
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
981-1105 |
8.82e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.97 E-value: 8.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 981 QLQAARERAR----------QQQEELRRKLQEIQRKKQ----------QEAAERAEAEKQRQK----ELEM-QL-AEEQK 1034
Cdd:PRK10929 124 QAQQEQDRAReisdslsqlpQQQTEARRQLNEIERRLQtlgtpntplaQAQLTALQAESAALKalvdELELaQLsANNRQ 203
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355871 1035 RLMEMAEE------ERLEYQQQKLaaeekaRQEAEERRKQEeeaAKLALEEATKLAQEQIRQKAALDKHLHFHQELS 1105
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 ... |
847-1081 |
9.53e-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: 9.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 847 QLSLELDALESQVaidgrLSSIQATDVASDMECEEERSHEDPSKaLQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQE 926
Cdd:pfam02463 268 AQVLKENKEEEKE-----KKLQEEELKLLAKEEEELKSELLKLE-RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 927 ELTWLHKEQLEKAEKMKEEleLEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAAR----ERARQQQEELRRKLQE 1002
Cdd:pfam02463 342 KELKELEIKREAEEEEEEE--LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELkseeEKEAQLLLELARQLED 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1003 IQRKKQQEAAERAEAEKQRQKELEMQLAEEQ-KRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEAT 1081
Cdd:pfam02463 420 LLKEEKKEELEILEEEEESIELKQGKLTEEKeELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERS 499
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
848-1119 |
1.02e-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: 46.76 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 848 LSLELDALESQVAidgrlSSIQATDVASDMECEEERSHEDPSKALQD------KKQQEKASRDRIRIEKAEMRWLK---- 917
Cdd:pfam12128 263 LHFGYKSDETLIA-----SRQEERQETSAELNQLLRTLDDQWKEKRDelngelSAADAAVAKDRSELEALEDQHGAflda 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 918 -VEQRRREQEELTwLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRlqlQAARERARQQQEEL 996
Cdd:pfam12128 338 dIETAAADQEQLP-SWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKL---AKIREARDRQLAVA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 997 RRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLME-MAEEERLEYQQQKLAAEEKARQEAEERRKQ------E 1069
Cdd:pfam12128 414 EDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQaTATPELLLQLENFDERIERAREEQEAANAEverlqsE 493
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355871 1070 EEAAKLALEEAT-KLAQEQIR---QKAALDKHLH--------FHQELSKEASGlqWTQNISR 1119
Cdd:pfam12128 494 LRQARKRRDQASeALRQASRRleeRQSALDELELqlfpqagtLLHFLRKEAPD--WEQSIGK 553
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
878-1108 |
1.03e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 46.50 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 878 ECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEEN 957
Cdd:pfam02463 195 LKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKEN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 958 RLRKQRLEEERQQQEEAEKKRRlQLQAARERARQQQEELRRKLQEIQR---------KKQQEAAERAEAEKQRQ--KELE 1026
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEE-ELKSELLKLERRKVDDEEKLKESEKekkkaekelKKEKEEIEELEKELKELeiKREA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1027 MQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRkqEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSK 1106
Cdd:pfam02463 354 EEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK--EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEI 431
|
..
gi 1720355871 1107 EA 1108
Cdd:pfam02463 432 LE 433
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
976-1107 |
1.17e-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: 46.38 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 976 KKRRLQLQAARerarQQQEELRRKL-----------QEIQRKKQ-----QEAAERAEAEKQRQKE--------------- 1024
Cdd:pfam09726 405 KKLKAELQASR----QTEQELRSQIssltslerslkSELGQLRQendllQTKLHNAVSAKQKDKQtvqqlekrlkaeqea 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1025 ---LEMQLAEEQKRLMEmaEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFH 1101
Cdd:pfam09726 481 rasAEKQLAEEKKRKKE--EEATAARAVALAAASRGECTESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQELRKY 558
|
....*.
gi 1720355871 1102 QELSKE 1107
Cdd:pfam09726 559 KESEKD 564
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
977-1075 |
1.23e-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: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 977 KRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEyqQQKLAAEE 1056
Cdd:pfam20492 13 ERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLE--AELAEAQE 90
|
90
....*....|....*....
gi 1720355871 1057 KARQEAEERRKQEEEAAKL 1075
Cdd:pfam20492 91 EIARLEEEVERKEEEARRL 109
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
976-1093 |
1.26e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.80 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 976 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAE 1055
Cdd:COG3064 44 LAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAE 123
|
90 100 110
....*....|....*....|....*....|....*...
gi 1720355871 1056 EKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1093
Cdd:COG3064 124 EAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAA 161
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1019-1093 |
1.52e-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: 1.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355871 1019 KQRQKELEMQLAEEQKRLMEM---AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1093
Cdd:cd06503 43 EKAKEEAEELLAEYEEKLAEAraeAQEIIEEARKEAEKIKEEILAEAKEEAERILEQAKAEIEQEKEKALAELRKEVA 120
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
983-1108 |
1.56e-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: 45.29 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 983 QAARERARQQQEELRRKLQEIQRKK--QQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQ 1060
Cdd:pfam13868 19 KCNKERDAQIAEKKRIKAEEKEEERrlDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1720355871 1061 EAEERRK-------QEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEA 1108
Cdd:pfam13868 99 EREQMDEiveriqeEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREE 153
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
893-1084 |
1.86e-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: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 893 QDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEEltWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQE 972
Cdd:TIGR00618 208 LCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH--AYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQER 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 973 EAEKKRRLQL---QAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQkrLMEMAEEERLEYQQ 1049
Cdd:TIGR00618 286 INRARKAAPLaahIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT--LHSQEIHIRDAHEV 363
|
170 180 190
....*....|....*....|....*....|....*
gi 1720355871 1050 QKLAAEEKARQEAEERRKQEEEAAKLALEEATKLA 1084
Cdd:TIGR00618 364 ATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSL 398
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
899-1112 |
1.95e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 899 EKASRDRIRIEKAEMRWLK-----VEQRRREQEELTWL--HKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQ 971
Cdd:COG4913 220 EPDTFEAADALVEHFDDLEraheaLEDAREQIELLEPIreLAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 972 EEAEKKRrlqLQAARERARQQQEELRRKLQEIQRKKQQEAAeraeaekQRQKELEMQLAEEQKRLMEmAEEERLEYQQQK 1051
Cdd:COG4913 300 LRAELAR---LEAELERLEARLDALREELDELEAQIRGNGG-------DRLEQLEREIERLERELEE-RERRRARLEALL 368
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355871 1052 LAAEEKARQEAEE--RRKQEEEAAKLALEEATKLAQEQIRQ-KAALDKHLHFHQELSKEASGLQ 1112
Cdd:COG4913 369 AALGLPLPASAEEfaALRAEAAALLEALEEELEALEEALAEaEAALRDLRRELRELEAEIASLE 432
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
842-1098 |
2.09e-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: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 842 HSAAGQLSLELDALESQVAIDGRLSSIQATDVASDMECE--EERSHEDPSKALQDKKQQEKasrDRIRIEKAEMRWLKVE 919
Cdd:TIGR00618 416 TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEklEKIHLQESAQSLKEREQQLQ---TKEQIHLQETRKKAVV 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 920 -QRRREQEELTWLHKEQLekaekMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRR 998
Cdd:TIGR00618 493 lARLLELQEEPCPLCGSC-----IHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQE 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 999 KLQEIQRKKQQEAAERAEAEKQRQKELEMQ-LAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEA-AKLA 1076
Cdd:TIGR00618 568 IQQSFSILTQCDNRSKEDIPNLQNITVRLQdLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAlKLTA 647
|
250 260
....*....|....*....|...
gi 1720355871 1077 LE-EATKLAQEQIRQKAALDKHL 1098
Cdd:TIGR00618 648 LHaLQLTLTQERVREHALSIRVL 670
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1019-1093 |
3.57e-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: 3.57e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355871 1019 KQRQKELEMQLAEEQKRLMEM---AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1093
Cdd:COG0711 44 ERAKEEAEAALAEYEEKLAEAraeAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAEAEIEQERAKALAELRAEVA 121
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
877-1091 |
3.78e-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: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 877 MECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRwLKVEQRRREQEELTWLHKEQLEKaekmkeelelEQQRRTEE 956
Cdd:pfam13868 82 IEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAE-EKLEKQRQLREEIDEFNEEQAEW----------KELEKEEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 957 NRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQeELRRKLQEIQRKKQQE----AAERAEAEKQRQKELEMQLAEE 1032
Cdd:pfam13868 151 REEDERILEYLKEKAEREEEREAEREEIEEEKEREIA-RLRAQQEKAQDEKAERdelrAKLYQEEQERKERQKEREEAEK 229
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355871 1033 QKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQK 1091
Cdd:pfam13868 230 KARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKR 288
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
970-1074 |
3.99e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 970 QQEEAEKKRRLQLQAARERARQQQEELRRKLQEiQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEM-AEEERLEYQ 1048
Cdd:PRK11637 170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYE-QQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELrANESRLRDS 248
|
90 100 110
....*....|....*....|....*....|.
gi 1720355871 1049 QQKLAAEEKARQEAEER-----RKQEEEAAK 1074
Cdd:PRK11637 249 IARAEREAKARAEREAReaarvRDKQKQAKR 279
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
880-1112 |
5.18e-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: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 880 EEERSHEdpsKALQ-DKKQQEKASRDRIRIEKAEMrwlkVEQRRREQEELTWLHK--EQLEKAEKMKEELELEQQRRTEE 956
Cdd:TIGR02168 220 AELRELE---LALLvLRLEELREELEELQEELKEA----EEELEELTAELQELEEklEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 957 NRLRKQRLEEERqqqeEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKqqeaaeraeaeKQRQKELEmQLAEEQKRL 1036
Cdd:TIGR02168 293 LANEISRLEQQK----QILRERLANLERQLEELEAQLEELESKLDELAEEL-----------AELEEKLE-ELKEELESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1037 MEMAEEERLEYQQQklaaeEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAAL----DKHLHFHQELSKEASGLQ 1112
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 ... |
859-1121 |
5.40e-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: 5.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 859 VAIDGRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKA-SRDRIRIEKAEMRwLKVEQRRREQEELTWLHKEQLE 937
Cdd:TIGR02794 41 VLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQrAAEQARQKELEQR-AAAEKAAKQAEQAAKQAEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 938 KAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQqeaaeraea 1017
Cdd:TIGR02794 120 QAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAK--------- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1018 ekqrqkelemqlAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKqeeeAAKLALEEATKLAQEQIRQKAALDKH 1097
Cdd:TIGR02794 191 ------------AEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERK----ADEAELGDIFGLASGSNAEKQGGARG 254
|
250 260
....*....|....*....|....*.
gi 1720355871 1098 LHFHQELSKEASGLQWT--QNISRPW 1121
Cdd:TIGR02794 255 AAAGSEVDKYAAIIQQAiqQNLYDDP 280
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
976-1112 |
7.06e-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: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 976 KKRRLQLQAARERARQQQEELRRKLQEIQrKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEM---------------- 1039
Cdd:COG4942 47 KKEEKALLKQLAALERRIAALARRIRALE-QELAALEAELAELEKEIAELRAELEAQKEELAELlralyrlgrqpplall 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1040 ---------------------AEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHL 1098
Cdd:COG4942 126 lspedfldavrrlqylkylapARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE 205
|
170
....*....|....
gi 1720355871 1099 HFHQELSKEASGLQ 1112
Cdd:COG4942 206 KELAELAAELAELQ 219
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
976-1096 |
7.14e-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: 7.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 976 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraeAEKQRQKELEMQLAEEQKRLMEMAEEErleyqqqklAAE 1055
Cdd:COG0711 44 ERAKEEAEAALAEYEEKLAEARAEAAEIIAEARK-------EAEAIAEEAKAEAEAEAERIIAQAEAE---------IEQ 107
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1720355871 1056 EKARQEAEERrkqeEEAAKLALEEATKLAQEQI---RQKAALDK 1096
Cdd:COG0711 108 ERAKALAELR----AEVADLAVAIAEKILGKELdaaAQAALVDR 147
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
847-1096 |
7.64e-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: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 847 QLSLELDALESQ-VAIDGRLSSIQATDVasdmECEEERshEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVE----QR 921
Cdd:TIGR02168 751 QLSKELTELEAEiEELEERLEEAEEELA----EAEAEI--EELEAQIEQLKEELKALREALDELRAELTLLNEEaanlRE 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 922 RREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQ 1001
Cdd:TIGR02168 825 RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1002 EIQRKKQQEAAERAeaeKQRQK---------ELEMQLAEEQKRLMEMAEEErLEYQQQKLAAEEKARQEAEERRKQEEEA 1072
Cdd:TIGR02168 905 ELESKRSELRRELE---ELREKlaqlelrleGLEVRIDNLQERLSEEYSLT-LEEAEALENKIEDDEEEARRRLKRLENK 980
|
250 260 270
....*....|....*....|....*....|....
gi 1720355871 1073 AK-------LALEEATKLAQEQI---RQKAALDK 1096
Cdd:TIGR02168 981 IKelgpvnlAAIEEYEELKERYDfltAQKEDLTE 1014
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
758-1092 |
8.31e-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: 8.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 758 HQAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELTPKKEKLGRKMKRTHKERNMEMAAGLSKSDITNSKEAGGTSHQG 837
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 838 LLRSHSAAGQLSLELDALESQVAIDGRLSSIQATDVASDMECEEE----------RSHEDPSKALQDKKQQEKASRDRIR 907
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaaalqnivvEDDEVAAAAIEYLKAAKAGRATFLP 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 908 IEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKKRRLQLQAARE 987
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 988 RARQQQEELRRKLQEIQRKKQQEAAE--RAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEER 1065
Cdd:COG1196 659 GGSLTGGSRRELLAALLEAEAELEELaeRLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELL 738
|
330 340
....*....|....*....|....*..
gi 1720355871 1066 RKQEEEAAKLALEEATKLAQEQIRQKA 1092
Cdd:COG1196 739 EELLEEEELLEEEALEELPEPPDLEEL 765
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
994-1096 |
9.14e-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: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 994 EELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMaeEERLEYQQQKLAAEEKARQEAEERRKQEEEaa 1073
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEAL--KARWEAEKELIEEIQELKEELEQRYGKIPE-- 489
|
90 100
....*....|....*....|...
gi 1720355871 1074 klaLEEATKLAQEQIRQKAALDK 1096
Cdd:COG0542 490 ---LEKELAELEEELAELAPLLR 509
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
976-1077 |
9.16e-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: 9.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 976 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeAAERAEAEKQRQKELEMQLAEEQKRLMEM-AEEERLEYQQQKLAA 1054
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAA-LEALKAERQKLLARLEKELAELAAELAELqQEAEELEALIARLEA 234
|
90 100
....*....|....*....|...
gi 1720355871 1055 EEKARQEAEERRKQEEEAAKLAL 1077
Cdd:COG4942 235 EAAAAAERTPAAGFAALKGKLPW 257
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
976-1091 |
9.43e-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: 9.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 976 KKRRLQLQAARERARQQQEELRRKLQEIQRKkqqeaaeraeaEKQRQKELEMQLAEEQKRLMEMAE-EERLEYQQQKLAA 1054
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRK-----------IGEIEKEIEQLEQEEEKLKERLEElEEDLSSLEQEIEN 755
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1720355871 1055 EEKARQEAEER-RKQEEEAAKLALEEAT---KLAQEQIRQK 1091
Cdd:TIGR02169 756 VKSELKELEARiEELEEDLHKLEEALNDleaRLSHSRIPEI 796
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
981-1109 |
9.76e-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: 9.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 981 QLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQ------RQKELEMQLAEEQKRLMEmAEEERLEYQQQkLAA 1054
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlarleaEVEQLEERIAQLSKELTE-LEAEIEELEER-LEE 772
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355871 1055 EEKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAAL-DKHLHFHQELSKEAS 1109
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtLLNEEAANLRERLES 828
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
983-1093 |
1.03e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.10 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 983 QAARERARQQQEELRRKLQEIQRK-----KQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEK 1057
Cdd:COG3064 11 EAAAQERLEQAEAEKRAAAEAEQKakeeaEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAE 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 1720355871 1058 ARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAA 1093
Cdd:COG3064 91 KKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAK 126
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
986-1093 |
1.24e-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: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 986 RERARQQQEELRRKLQEIQRKKQQEAAERaeaekQRQKELEMQLAEEQKRLMEmaEEERLEYQQQKL-----AAEEKARQ 1060
Cdd:pfam20492 1 REEAEREKQELEERLKQYEEETKKAQEEL-----EESEETAEELEEERRQAEE--EAERLEQKRQEAeeekeRLEESAEM 73
|
90 100 110
....*....|....*....|....*....|...
gi 1720355871 1061 EAEERRKQEEEAAklALEEATKLAQEQIRQKAA 1093
Cdd:pfam20492 74 EAEEKEQLEAELA--EAQEEIARLEEEVERKEE 104
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
847-1112 |
1.33e-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: 43.13 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 847 QLSLELDALESQVA-IDGRLSSIQATDVASDMECEEERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQ 925
Cdd:TIGR02169 748 SLEQEIENVKSELKeLEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 926 EELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEK---KRRLQLQAARERARQQQEELRRKLQE 1002
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRdleSRLGDLKKERDELEAQLRELERKIEE 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1003 IQRKKQQeaaeraeaEKQRQKELEMQLAEEQKRLMEM-AEEERLEYQQQKLAAEEKARQEaeerrKQEEEAAKLALEEAT 1081
Cdd:TIGR02169 908 LEAQIEK--------KRKRLSELKAKLEALEEELSEIeDPKGEDEEIPEEELSLEDVQAE-----LQRVEEEIRALEPVN 974
|
250 260 270
....*....|....*....|....*....|..
gi 1720355871 1082 KLA-QEQIRQKAALDKHLHFHQELSKEASGLQ 1112
Cdd:TIGR02169 975 MLAiQEYEEVLKRLDELKEKRAKLEEERKAIL 1006
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
976-1082 |
1.36e-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: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 976 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQR-----QKELEMQ------LAEEQKRLMEMAE--- 1041
Cdd:COG1579 44 EARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKeyealQKEIESLkrrisdLEDEILELMERIEele 123
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1720355871 1042 ------EERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATK 1082
Cdd:COG1579 124 eelaelEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
759-1109 |
1.40e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 759 QAKALKKEREERGLGQAEAAGGKPKHSKIKKKSELTPKKEKLGRKMKRTHKE------RNMEMAAGLSKS---DITNSKE 829
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEdknmalRKAEEAKKAEEArieEVMKLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 830 AGGTSHQGLLRSHSAAGQLSLELDALESQVAIDGRLSSIQATDV--ASDMECEEE----RSHEDPSKALQDKKQQEKASR 903
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkkAEELKKAEEenkiKAAEEAKKAEEDKKKAEEAKK 1682
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 904 DRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAekmkeelelEQQRRTEENRLRKQRleeerqqqeeaekkrrlQLQ 983
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA---------EELKKAEEENKIKAE-----------------EAK 1736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 984 AARERARQQQEELRRKLQEiQRKKQQEAAERAEAEKQRQKELEMQLAEEQKR---LMEMAEEERLEYQQQKLAAEEKARQ 1060
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEE-KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEedeKRRMEVDKKIKDIFDNFANIIEGGK 1815
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1720355871 1061 EAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEAS 1109
Cdd:PTZ00121 1816 EGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDG 1864
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
881-1107 |
1.48e-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: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 881 EERSHEDPSKALQDKKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELtwLHKEQLEKAEKMKEELELEQQRRTEENRLR 960
Cdd:TIGR00618 275 QEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRS--RAKLLMKRAAHVKQQSSIEEQRRLLQTLHS 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 961 KQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMA 1040
Cdd:TIGR00618 353 QEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQ 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1041 EEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQ-EQIRQKAALDK--HLHFHQELSKE 1107
Cdd:TIGR00618 433 QELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTkEQIHLQETRKKavVLARLLELQEE 502
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
976-1082 |
1.67e-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: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 976 KKRRLQLQAARERARQQQE--------ELRRKLQEiQRKKQqeaaeraeaekQRQKELEMQLAEEQKRLMEMAEEERLEY 1047
Cdd:pfam07767 209 KKRLKEEEKLERVLEKIAEsaataearEEKRKTKA-QRNKE-----------KRRKEEEREAKEEKALKKKLAQLERLKE 276
|
90 100 110
....*....|....*....|....*....|....*
gi 1720355871 1048 QQQKLAAEEKARQEAEERRKQEEEAAKLALEEATK 1082
Cdd:pfam07767 277 IAKEIAEKEKEREEKAEARKREKRKKKKEEKKLRP 311
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
895-1091 |
1.92e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 895 KKQQEKASRDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEA 974
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 975 EKKRRLQLQAarERARQQQEELRRKLQEIQRKkqqeaaeraeaeKQRQKELEMQLAEEQKRLMEMAEEERLeYQQQKLAA 1054
Cdd:PRK03918 307 DELREIEKRL--SRLEEEINGIEERIKELEEK------------EERLEELKKKLKELEKRLEELEERHEL-YEEAKAKK 371
|
170 180 190
....*....|....*....|....*....|....*..
gi 1720355871 1055 EEKARQEAEERRKQEEEAAKLaLEEATKlAQEQIRQK 1091
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKE-LEELEK-AKEEIEEE 406
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
880-1103 |
2.67e-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: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 880 EEERSHEDPSKALQDKKQQEKAS-RDRIRIEKAEMRWLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQqrrTEENR 958
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHkRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQ---AELNR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 959 LRKQRLEEERQQQeeaeKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraEAEKQRQKELEMQLAEEQKRLME 1038
Cdd:pfam05557 80 LKKKYLEALNKKL----NEKESQLADAREVISCLKNELSELRRQIQRAELE------LQSTNSELEELQERLDLLKAKAS 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355871 1039 MAEE--ERLEYQQQKLAAEEKARQEAEERRKQEEEAAklaleEATKLAQEQIRQKAALDKHLHFHQE 1103
Cdd:pfam05557 150 EAEQlrQNLEKQQSSLAEAEQRIKELEFEIQSQEQDS-----EIVKNSKSELARIPELEKELERLRE 211
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
976-1087 |
2.70e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 976 KKRRLQLQAAR-ERARQQQEELRRKLQEIQRK-KQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKla 1053
Cdd:PRK00409 528 LERELEQKAEEaEALLKEAEKLKEELEEKKEKlQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVK-- 605
|
90 100 110
....*....|....*....|....*....|....
gi 1720355871 1054 aeekaRQEAEERRKQEEEAAKLALEEATKLAQEQ 1087
Cdd:PRK00409 606 -----AHELIEARKRLNKANEKKEKKKKKQKEKQ 634
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
978-1108 |
2.72e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.44 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 978 RRLQLQAARERARQQQEELRRKLQEIQRKKQQEAA-----ERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKL 1052
Cdd:pfam13868 43 RRLDEMMEEERERALEEEEEKEEERKEERKRYRQEleeqiEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKL 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355871 1053 AAEEKARQEAEE------RRKQEEeaaKLALEEATKLAQEQIRQKAALDKHLHFHQELSKEA 1108
Cdd:pfam13868 123 EKQRQLREEIDEfneeqaEWKELE---KEEEREEDERILEYLKEKAEREEEREAEREEIEEE 181
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
976-1098 |
3.39e-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: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 976 KKRRLQLQAARERARQQQEELRRKLQEIQ--------RKKQQEAAERAEAEKQRQKELEMQ------LAEEQKRLMEMAE 1041
Cdd:COG1579 41 AALEARLEAAKTELEDLEKEIKRLELEIEevearikkYEEQLGNVRNNKEYEALQKEIESLkrrisdLEDEILELMERIE 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355871 1042 EERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLAlEEATKLAQEQIRQKAALDKHL 1098
Cdd:COG1579 121 ELEEELAELEAELAELEAELEEKKAELDEELAELE-AELEELEAEREELAAKIPPEL 176
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
992-1108 |
3.55e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 40.77 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 992 QQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEE 1071
Cdd:PRK06669 31 SIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEEAKEELLKKTDEASSIIEKLQMQIEREQEEWEE 110
|
90 100 110
....*....|....*....|....*....|....*..
gi 1720355871 1072 AAKLALEEATKLAQEQIRQKaALDKHLHFHQELSKEA 1108
Cdd:PRK06669 111 ELERLIEEAKAEGYEEGYEK-GREEGLEEVRELIEQL 146
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
980-1094 |
3.81e-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: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 980 LQLQAARERA-RQQQEELRRKLQEIQRKKQQEAAEraeaeKQRQKELEMQLAEEQKRLMEMaeEERLEYQQQKLaaEEKA 1058
Cdd:cd16269 176 LQSKEAEAEAiLQADQALTEKEKEIEAERAKAEAA-----EQERKLLEEQQRELEQKLEDQ--ERSYEEHLRQL--KEKM 246
|
90 100 110
....*....|....*....|....*....|....*.
gi 1720355871 1059 RQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAAL 1094
Cdd:cd16269 247 EEERENLLKEQERALESKLKEQEALLEEGFKEQAEL 282
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
983-1078 |
4.31e-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: 40.35 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 983 QAARERARQQQEELRRKLQEIQRKKQQEaaeraeaeKQRQKELEMQLAEEqkrlMEMaEEERLEYQQQKLAAEEKARQEA 1062
Cdd:pfam02841 210 RAKAEAAEAEQELLREKQKEEEQMMEAQ--------ERSYQEHVKQLIEK----MEA-EREQLLAEQERMLEHKLQEQEE 276
|
90
....*....|....*.
gi 1720355871 1063 EERRKQEEEAAKLALE 1078
Cdd:pfam02841 277 LLKEGFKTEAESLQKE 292
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
983-1090 |
4.51e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 41.09 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 983 QAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQ--KELEMQLAEEQKRLmemaeEERLEYQQQKlaAEEKARQ 1060
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELValEGLAAELEEKQQEL-----EAQLEQLQEK--AAETSQE 213
|
90 100 110
....*....|....*....|....*....|...
gi 1720355871 1061 EAEERRKQEEEAAK-LALEEAT--KLAQEQIRQ 1090
Cdd:PRK11448 214 RKQKRKEITDQAAKrLELSEEEtrILIDQQLRK 246
|
|
| 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 ... |
996-1093 |
5.04e-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: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 996 LRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLME-MAEEERLEYQQQKLAAE--EKARQEAEERRKQEEEA 1072
Cdd:pfam00430 20 AWKPLGKVLDKRRELIADEIAEAEERRKDAAAALAEAEQQLKEaRAEAQEIIENAKKRAEKlkEEIVAAAEAEAERIIEQ 99
|
90 100
....*....|....*....|.
gi 1720355871 1073 AKLALEEATKLAQEQIRQKAA 1093
Cdd:pfam00430 100 AAAEIEQEKDRALAELRQQVV 120
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1019-1095 |
5.28e-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: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 1019 KQRQKELEMQLAEEQKRLMEMaeEERLEYQQQKLAaeeKARQEAEERRKQEEEAAKLALEEATKLAQ---EQIRQKAALD 1095
Cdd:cd06503 29 DEREEKIAESLEEAEKAKEEA--EELLAEYEEKLA---EARAEAQEIIEEARKEAEKIKEEILAEAKeeaERILEQAKAE 103
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
983-1071 |
5.37e-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: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 983 QAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEM---QLAEEQKRLMEmaeeerLEYQQQKLAAEEKAR 1059
Cdd:cd16269 204 RAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEereNLLKEQERALE------SKLKEQEALLEEGFK 277
|
90
....*....|..
gi 1720355871 1060 QEAEERRKQEEE 1071
Cdd:cd16269 278 EQAELLQEEIRS 289
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
917-1092 |
6.40e-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: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 917 KVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEaekKRRLQLQAARER-------- 988
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE---REIAELEAELERldassddl 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 989 --ARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQkelemQLAEEQKRLMEMAEE-ERLEYQQQKLAAEEKARQEAEER 1065
Cdd:COG4913 688 aaLEEQLEELEAELEELEEELDELKGEIGRLEKELE-----QAEEELDELQDRLEAaEDLARLELRALLEERFAAALGDA 762
|
170 180
....*....|....*....|....*..
gi 1720355871 1066 RkqeEEAAKLALEEATKLAQEQIRQKA 1092
Cdd:COG4913 763 V---ERELRENLEERIDALRARLNRAE 786
|
|
| RIB43A |
pfam05914 |
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar ... |
901-1098 |
6.97e-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: 40.27 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 901 ASRDRIRIEKAEMR-WLKVEQRRREQEELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEerqqqeeaekKRR 979
Cdd:pfam05914 141 NREERKKLQQEQMReWLEQQIEEKKQAEEEEKHAELLYDQKRLERDRRALELAKLEEECRRAVNAAT----------KNF 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 980 LQLQAARERARQQQEELRR---KLQEIQ---------RKKQQEAAER--------------AEAEKQRQKELEMQLAEEQ 1033
Cdd:pfam05914 211 NQALAAEQAERRRLEKRQEqedNLAEIYnhltsdlltENPEVAQSSLgphrvipdrwkgmsPEQLKEIRKEQEQQREEKE 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720355871 1034 KRLMEMAEEERLEYQQQKLAAEEKARQEAEERRKQEEEAAKLAlEEATKLAQEQIRQKAALDKHL 1098
Cdd:pfam05914 291 RRREEEKQRDAEWDRQRLELARAALLLEREQQRLRRELRRQLD-EENLQLAQEQKARQEYLNKEV 354
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
876-1090 |
7.23e-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: 40.02 E-value: 7.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 876 DMECEEERSHEDPSKALQDKK------QQEKASRDRIR--IEKAEMRWLKVEQRRREQEELTWLHKEQ--------LEKA 939
Cdd:pfam15558 75 GREERRRADRREKQVIEKESRwreqaeDQENQRQEKLEraRQEAEQRKQCQEQRLKEKEEELQALREQnslqlqerLEEA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 940 EKMKEELELEQQRR-TEENRLRKQRLEEERQQQEEAEKKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAE 1018
Cdd:pfam15558 155 CHKRQLKEREEQKKvQENNLSELLNHQARKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEERHRELREKAQKEEEQ 234
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355871 1019 KQRQKELEMQLAEEQKRLMEM-AEEERLEYQQQKLAAEEKARQEAEERRKQEEE------AAKLALEEATKLAQEQIRQ 1090
Cdd:pfam15558 235 FQRAKWRAEEKEEERQEHKEAlAELADRKIQQARQVAHKTVQDKAQRARELNLEreknhhILKLKVEKEEKCHREGIKE 313
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
899-1112 |
7.29e-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: 40.02 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 899 EKASRDRIRIEKAEMRWlkVEQRRREQE-ELTWLHKEQLEKAEKMKEELELEQQRRTEENRLRKQRLEEERQQQEEAEKK 977
Cdd:pfam15558 18 KEEQRMRELQQQAALAW--EELRRRDQKrQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 978 RRLQLQAaRERARQ-------QQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERL-EYQQ 1049
Cdd:pfam15558 96 WREQAED-QENQRQeklerarQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVqENNL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355871 1050 QKLAAEEKARQEAEERRKQEEEAAKLALEEATKLAQEqIRQKAALDKHLHFHQELSKEASGLQ 1112
Cdd:pfam15558 175 SELLNHQARKVLVDCQAKAEELLRRLSLEQSLQRSQE-NYEQLVEERHRELREKAQKEEEQFQ 236
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
976-1098 |
7.83e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 976 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAeKQRQKELEmQLAEEQKRLMEMAEEERLEYQQQKLAAE 1055
Cdd:COG4372 69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA-EELQEELE-ELQKERQDLEQQRKQLEAQIAELQSEIA 146
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1720355871 1056 EKARQEAEERRKQEEEAAKLALEEATKLAQEQIRQKAALDKHL 1098
Cdd:COG4372 147 EREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
976-1092 |
7.86e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 40.02 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 976 KKRRLQLQAARERARQQQEELRRKLQEIQRK-KQQEAAERAEAEKQRQKelemQLAEEQKRLMEmAEEERLEYQQQKLAA 1054
Cdd:COG3064 22 EAEKRAAAEAEQKAKEEAEEERLAELEAKRQaEEEAREAKAEAEQRAAE----LAAEAAKKLAE-AEKAAAEAEKKAAAE 96
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1720355871 1055 EEKARQEAEE---RRKQEEEAAKLALEEATKLAQEQIRQKA 1092
Cdd:COG3064 97 KAKAAKEAEAaaaAEKAAAAAEKEKAEEAKRKAEEEAKRKA 137
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
976-1085 |
8.08e-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: 8.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 976 KKRRLQLQAARERARQQQEELRRKLQEIQRKKQQeaaeraeaEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAE 1055
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAELEAQQAE--------QEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
90 100 110
....*....|....*....|....*....|
gi 1720355871 1056 EKARQEAEERRKQEEEAAKLALEEATKLAQ 1085
Cdd:COG3883 218 AAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
977-1096 |
8.99e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 40.13 E-value: 8.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355871 977 KRRLQlQAARERARQQQEELRRKLQEIQRKKQQEAAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQQQKLAAEE 1056
Cdd:pfam09731 293 HREID-QLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIRESYEEKLRTELE 371
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1720355871 1057 KARQEAEERRKQEEEAAKLALEEA------TKLAQEQIRQKAALDK 1096
Cdd:pfam09731 372 RQAEAHEEHLKDVLVEQEIELQREflqdikEKVEEERAGRLLKLNE 417
|
|
|