|
Name |
Accession |
Description |
Interval |
E-value |
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
210-524 |
5.14e-52 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 181.40 E-value: 5.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 210 GAFEVQSRAVESTTSFSGRFrPGDVITLVSPFESTVVARHVEYGERVDEGDLLLELDSTEIDIRYRRARSDLADAESELE 289
Cdd:COG1566 22 ALWAAGRNGPDEPVTADGRV-EARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 290 DLE-DWEQGREMASSRRSLRQAERNLSNDQRELDDVEHLFERGIVPERELRAARERVEESRVRVEAAREDLAETSRQGGE 368
Cdd:COG1566 101 RLEaELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLRE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 369 RA-IARARVEVENARAEYEQVQRQRDGARVYAPVDGVVLaplgeDRddgeRVEAGGRVSSGAALLAVGDLSSLEIEGTVD 447
Cdd:COG1566 181 EEeLAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVT-----NL----NVEPGEVVSAGQPLLTIVPLDDLWVEAYVP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 448 ELDIHDVQAGQSARVNVVRGGGDPMPARVSYVSSQAQEGSGRGLPSFRLV----VRIdDLDDQDLERIRVGMSASVDVIT 523
Cdd:COG1566 252 ETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTSPPKNATGNVVqrypVRI-RLDNPDPEPLRPGMSATVEIDT 330
|
.
gi 648489684 524 Q 524
Cdd:COG1566 331 E 331
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
211-580 |
3.26e-28 |
|
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 273776 [Multi-domain] Cd Length: 322 Bit Score: 115.10 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 211 AFEVQSRAVESTTSFSGRFRPGDVITLVSPFESTVVARHVEYGERVDEGDLLLELDSTEIDIRYRRARSDLADAESELED 290
Cdd:TIGR01730 3 VATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 291 ledweqgremasSRRSLRQAERnlsndqrelddvehLFERGIVPERELRAARERVEESRVRVEAAREDLAetsrqggera 370
Cdd:TIGR01730 83 ------------AQRSFERAER--------------LVKRNAVSQADLDDAKAAVEAAQADLEAAKASLA---------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 371 iararveveNARAEYEQvqrqrdgARVYAPVDGVVlaplgedrddGER-VEAGGRVSSGAALLAVGDLSSLEIEGTVDEL 449
Cdd:TIGR01730 127 ---------SAQLNLRY-------TEIRAPFDGTI----------GRRlVEVGAYVTAGQTLATIVDLDPLEADFSVPER 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 450 DIHDVQAGQSARVNVVRGGGDPMPARVSYVSSQAQEGSGrglpSFRLVVRIDDLDdqdlERIRVGMSASVDVITQQDSDA 529
Cdd:TIGR01730 181 DLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTG----TVRVRATFPNPD----GRLLPGMFGRVTISLKVRSSA 252
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 648489684 530 VVVPHAYL--GGSGSERWVLRQtSNGSERIAVELGRSRYDGVQVRSGVEPGDR 580
Cdd:TIGR01730 253 IVVPTQAVieDLNGKYVYVVKN-DGKVSKRPVEVGLRNGGYVEIESGLKAGDQ 304
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
1-131 |
8.47e-16 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 79.12 E-value: 8.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 1 MSDSPVMLsQQILDSMADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFIGEEgyaAFVDALFEAVYSGVMQP 80
Cdd:COG3852 2 LRESEELL-RAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDS---PLRELLERALAEGQPVT 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 648489684 81 DQMVSI-SVGGHVRSLKLTTSYLapRQAGGERAVLAVFTDVTDL----EQARQAEQ 131
Cdd:COG3852 78 EREVTLrRKDGEERPVDVSVSPL--RDAEGEGGVLLVLRDITERkrleRELRRAEK 131
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
218-523 |
9.23e-14 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 72.46 E-value: 9.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 218 AVESTTSFSGRFRPGDVITLVSPFESTVVAR-HVEYGERVDEGDLLLELDSTEIDIRYRRARSDLADA-------ESELE 289
Cdd:pfam00529 3 PLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRvLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAqaqvarlQAELD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 290 DLEDWEQGR------------EMASSRRSLRQAERNLSNDQRELDDVEHLFERGIVPERELRAARERVEESRVRVEAARE 357
Cdd:pfam00529 83 RLQALESELaisrqdydgataQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 358 DLA----------ETSRQGGERAIARARVEVENARAEYEQVQRQRDGARVYAPVDGVVLaplgedrDDGERVEaGGRVSS 427
Cdd:pfam00529 163 QLDqiyvqitqsaAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVA-------FLSVTVD-GGTVSA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 428 GAALLAVGDLSSLEIEGTVDELDIHDVQAGQSARVNVVRGGGDPMPARVSYVSSQAQEGSGRGLpsfrlvvrIDDLDDQD 507
Cdd:pfam00529 235 GLRLMFVVPEDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRV--------VVDKAQGP 306
|
330
....*....|....*.
gi 648489684 508 LERIRVGMSASVDVIT 523
Cdd:pfam00529 307 YYPLRIGLSAGALVRL 322
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
8-130 |
4.26e-13 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 71.92 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 8 LSQQILDSMADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFIGEegyAAFVDALFEAVYSGVMQPDQMVSIS 87
Cdd:PRK11360 263 LNELILESIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPPN---TPFASPLLDTLEHGTEHVDLEISFP 339
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 648489684 88 VGGHVRSLKLTTSYLAPRQAGGERAVLaVFTDVTDL----EQARQAE 130
Cdd:PRK11360 340 GRDRTIELSVSTSLLHNTHGEMIGALV-IFSDLTERkrlqRRVARQE 385
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
232-531 |
9.53e-11 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 63.94 E-value: 9.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 232 GDVITLVSPFESTVVARHVEYGERVDEGDLLLELDSTEIDIRYRRARSDLADAESELEDLedweqgreMASSRR-----S 306
Cdd:PRK15136 59 GNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTALANSVRQTHQL--------MINSKQyqaniE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 307 LRQAErnLSNDQRELDDVEHLFERGIVPERELRAARERVEESRVRVEAAREDLAetSRQG--------GERAIARARVEV 378
Cdd:PRK15136 131 LQKTA--LAQAQSDLNRRVPLGNANLIGREELQHARDAVASAQAQLDVAIQQYN--ANQAmilntpleDQPAVQQAATEV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 379 ENAraeYEQVQRqrdgARVYAPVDGVVlaplgedrddGER-VEAGGRVSSGAALLAVGDLSSLEIEGTVDELDIHDVQAG 457
Cdd:PRK15136 207 RNA---WLALQR----TKIVSPMTGYV----------SRRsVQVGAQISPTTPLMAVVPATNLWVDANFKETQLANMRIG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 458 QSARV-------NVVRGG---GDPMPARVSYVSSQAQEGSGRGLPSF-RLVVRIdDLDDQDLER--IRVGMSASVDVITq 524
Cdd:PRK15136 270 QPATItsdiygdDVVYTGkvvGLDMGTGSAFSLLPAQNATGNWIKVVqRLPVRI-ELDAKQLAQhpLRIGLSTLVTVDT- 347
|
....*..
gi 648489684 525 QDSDAVV 531
Cdd:PRK15136 348 ANRDGQV 354
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
11-129 |
1.12e-10 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 59.23 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 11 QILDSMADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFigEEGYAAFVDALFEAVYSGVMQPDQM--VSISV 88
Cdd:TIGR00229 7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELI--PEEDREEVRERIERRLEGEPEPVSEerRVRRK 84
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 648489684 89 GGHVRSLKLTTSYLapRQAGGERAVLAVFTDVTDLEQARQA 129
Cdd:TIGR00229 85 DGSEIWVEVSVSPI--RTNGGELGVVGIVRDITERKEAEEA 123
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
10-120 |
9.12e-10 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 56.27 E-value: 9.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 10 QQILDSMADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFIgEEGYAAFVDALFEAVYSGvmQPDQMVSISVG 89
Cdd:pfam00989 4 RAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIP-EEDDAEVAELLRQALLQG--EESRGFEVSFR 80
|
90 100 110
....*....|....*....|....*....|....*
gi 648489684 90 ---GHVRSLKLTTSYLapRQAGGE-RAVLAVFTDV 120
Cdd:pfam00989 81 vpdGRPRHVEVRASPV--RDAGGEiLGFLGVLRDI 113
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
10-60 |
1.24e-08 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 51.63 E-value: 1.24e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 648489684 10 QQILDSMADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFIGEE 60
Cdd:smart00091 4 RAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPED 54
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
16-120 |
1.45e-05 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 44.16 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 16 MADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFIGEEgYAAFVDALFEAVYSGVMQPDQMVSISVGGHVRSL 95
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPED-REELRERLENLLSGGEPVTLEVRLRRKDGSVIWV 79
|
90 100
....*....|....*....|....*
gi 648489684 96 kLTTSYLAPRQAGGERAVLAVFTDV 120
Cdd:cd00130 80 -LVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
210-524 |
5.14e-52 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 181.40 E-value: 5.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 210 GAFEVQSRAVESTTSFSGRFrPGDVITLVSPFESTVVARHVEYGERVDEGDLLLELDSTEIDIRYRRARSDLADAESELE 289
Cdd:COG1566 22 ALWAAGRNGPDEPVTADGRV-EARVVTVAAKVSGRVTEVLVKEGDRVKKGQVLARLDPTDLQAALAQAEAQLAAAEAQLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 290 DLE-DWEQGREMASSRRSLRQAERNLSNDQRELDDVEHLFERGIVPERELRAARERVEESRVRVEAAREDLAETSRQGGE 368
Cdd:COG1566 101 RLEaELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLRE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 369 RA-IARARVEVENARAEYEQVQRQRDGARVYAPVDGVVLaplgeDRddgeRVEAGGRVSSGAALLAVGDLSSLEIEGTVD 447
Cdd:COG1566 181 EEeLAAAQAQVAQAEAALAQAELNLARTTIRAPVDGVVT-----NL----NVEPGEVVSAGQPLLTIVPLDDLWVEAYVP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 448 ELDIHDVQAGQSARVNVVRGGGDPMPARVSYVSSQAQEGSGRGLPSFRLV----VRIdDLDDQDLERIRVGMSASVDVIT 523
Cdd:COG1566 252 ETDLGRVKPGQPVEVRVDAYPDRVFEGKVTSISPGAGFTSPPKNATGNVVqrypVRI-RLDNPDPEPLRPGMSATVEIDT 330
|
.
gi 648489684 524 Q 524
Cdd:COG1566 331 E 331
|
|
| AcrA |
COG0845 |
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope ... |
214-581 |
1.76e-49 |
|
Multidrug efflux pump subunit AcrA (membrane-fusion protein) [Cell wall/membrane/envelope biogenesis, Defense mechanisms];
Pssm-ID: 440606 [Multi-domain] Cd Length: 324 Bit Score: 174.36 E-value: 1.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 214 VQSRAVESTTSFSGRFRPGDVITLVSPFESTVVARHVEYGERVDEGDLLLELDSTEIDIRYRRARSDLAdaeseledled 293
Cdd:COG0845 3 VERGDVPETVEATGTVEARREVEVRARVSGRVEEVLVDEGDRVKKGQVLARLDPPDLQAALAQAQAQLA----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 294 weqgremassrrslrQAERNLSNDQRELDDVEHLFERGIVPERELRAARERVEEsrvrveaaredlaetsrqggeraiar 373
Cdd:COG0845 72 ---------------AAQAQLELAKAELERYKALLKKGAVSQQELDQAKAALDQ-------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 374 ARVEVENARAEYEQVQRQRDGARVYAPVDGVVLAPLgedrddgerVEAGGRVSSGAALLAVGDLSSLEIEGTVDELDIHD 453
Cdd:COG0845 111 AQAALAAAQAALEQARANLAYTTIRAPFDGVVGERN---------VEPGQLVSAGTPLFTIADLDPLEVEFDVPESDLAR 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 454 VQAGQSARVNVVRGGGDPMPARVSYVSSQAQEGSGrglpSFRLVVRIDDLDDqdleRIRVGMSASVDVITQQDSDAVVVP 533
Cdd:COG0845 182 LKVGQPVTVTLDAGPGKTFEGKVTFIDPAVDPATR----TVRVRAELPNPDG----LLRPGMFVRVRIVLGERENALLVP 253
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 648489684 534 HAYLGGSGSERWVLRQTSNGS-ERIAVELGRSRYDGVQVRSGVEPGDRL 581
Cdd:COG0845 254 ASAVVRDGGGAYVFVVDADGKvERRPVTLGRRDGDQVEVLSGLKAGDRV 302
|
|
| RND_mfp |
TIGR01730 |
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion ... |
211-580 |
3.26e-28 |
|
RND family efflux transporter, MFP subunit; This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 273776 [Multi-domain] Cd Length: 322 Bit Score: 115.10 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 211 AFEVQSRAVESTTSFSGRFRPGDVITLVSPFESTVVARHVEYGERVDEGDLLLELDSTEIDIRYRRARSDLADAESELED 290
Cdd:TIGR01730 3 VATVESETLANTLTFPGSLEAVDEADLAAEVAGKITKISVREGQKVKKGQVLARLDDDDYQLALQAALAQLAAAEAQLEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 291 ledweqgremasSRRSLRQAERnlsndqrelddvehLFERGIVPERELRAARERVEESRVRVEAAREDLAetsrqggera 370
Cdd:TIGR01730 83 ------------AQRSFERAER--------------LVKRNAVSQADLDDAKAAVEAAQADLEAAKASLA---------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 371 iararveveNARAEYEQvqrqrdgARVYAPVDGVVlaplgedrddGER-VEAGGRVSSGAALLAVGDLSSLEIEGTVDEL 449
Cdd:TIGR01730 127 ---------SAQLNLRY-------TEIRAPFDGTI----------GRRlVEVGAYVTAGQTLATIVDLDPLEADFSVPER 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 450 DIHDVQAGQSARVNVVRGGGDPMPARVSYVSSQAQEGSGrglpSFRLVVRIDDLDdqdlERIRVGMSASVDVITQQDSDA 529
Cdd:TIGR01730 181 DLPQLRRGQTLTVELDALPGEEFKGKLRFIDPRVDSGTG----TVRVRATFPNPD----GRLLPGMFGRVTISLKVRSSA 252
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 648489684 530 VVVPHAYL--GGSGSERWVLRQtSNGSERIAVELGRSRYDGVQVRSGVEPGDR 580
Cdd:TIGR01730 253 IVVPTQAVieDLNGKYVYVVKN-DGKVSKRPVEVGLRNGGYVEIESGLKAGDQ 304
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
1-131 |
8.47e-16 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 79.12 E-value: 8.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 1 MSDSPVMLsQQILDSMADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFIGEEgyaAFVDALFEAVYSGVMQP 80
Cdd:COG3852 2 LRESEELL-RAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDS---PLRELLERALAEGQPVT 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 648489684 81 DQMVSI-SVGGHVRSLKLTTSYLapRQAGGERAVLAVFTDVTDL----EQARQAEQ 131
Cdd:COG3852 78 EREVTLrRKDGEERPVDVSVSPL--RDAEGEGGVLLVLRDITERkrleRELRRAEK 131
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
218-523 |
9.23e-14 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 72.46 E-value: 9.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 218 AVESTTSFSGRFRPGDVITLVSPFESTVVAR-HVEYGERVDEGDLLLELDSTEIDIRYRRARSDLADA-------ESELE 289
Cdd:pfam00529 3 PLTKGVEAPGRVVVSGNAKAVQPQVSGIVTRvLVKEGDRVKAGDVLFQLDPTDYQAALDSAEAQLAKAqaqvarlQAELD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 290 DLEDWEQGR------------EMASSRRSLRQAERNLSNDQRELDDVEHLFERGIVPERELRAARERVEESRVRVEAARE 357
Cdd:pfam00529 83 RLQALESELaisrqdydgataQLRAAQAAVKAAQAQLAQAQIDLARRRVLAPIGGISRESLVTAGALVAQAQANLLATVA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 358 DLA----------ETSRQGGERAIARARVEVENARAEYEQVQRQRDGARVYAPVDGVVLaplgedrDDGERVEaGGRVSS 427
Cdd:pfam00529 163 QLDqiyvqitqsaAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTEIRAPVDGTVA-------FLSVTVD-GGTVSA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 428 GAALLAVGDLSSLEIEGTVDELDIHDVQAGQSARVNVVRGGGDPMPARVSYVSSQAQEGSGRGLpsfrlvvrIDDLDDQD 507
Cdd:pfam00529 235 GLRLMFVVPEDNLLVPGMFVETQLDQVRVGQPVLIPFDAFPQTKTGRFTGVVVGISPDTGPVRV--------VVDKAQGP 306
|
330
....*....|....*.
gi 648489684 508 LERIRVGMSASVDVIT 523
Cdd:pfam00529 307 YYPLRIGLSAGALVRL 322
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
8-130 |
4.26e-13 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 71.92 E-value: 4.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 8 LSQQILDSMADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFIGEegyAAFVDALFEAVYSGVMQPDQMVSIS 87
Cdd:PRK11360 263 LNELILESIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPPN---TPFASPLLDTLEHGTEHVDLEISFP 339
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 648489684 88 VGGHVRSLKLTTSYLAPRQAGGERAVLaVFTDVTDL----EQARQAE 130
Cdd:PRK11360 340 GRDRTIELSVSTSLLHNTHGEMIGALV-IFSDLTERkrlqRRVARQE 385
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
10-164 |
9.77e-13 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 70.57 E-value: 9.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 10 QQILDSMADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFIGEegyaafvdALFEAVYSGvmQPDQMVSISVG 89
Cdd:COG3829 14 EAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNS--------PLLEVLKTG--KPVTGVIQKTG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648489684 90 GHVRSLKLTTSylaPRQAGGE-RAVLAVFTDVTDLEqarQAEQSLSDELRGKHKELQDAFLEIEANSEALQQAYRR 164
Cdd:COG3829 84 GKGKTVIVTAI---PIFEDGEvIGAVETFRDITELK---RLERKLREEELERGLSAKYTFDDIIGKSPAMKELLEL 153
|
|
| type_I_hlyD |
TIGR01843 |
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport ... |
219-523 |
3.05e-12 |
|
type I secretion membrane fusion protein, HlyD family; Type I secretion is an ABC transport process that exports proteins, without cleavage of any signal sequence, from the cytosol to extracellular medium across both inner and outer membranes. The secretion signal is found in the C-terminus of the transported protein. This model represents the adaptor protein between the ATP-binding cassette (ABC) protein of the inner membrane and the outer membrane protein, and is called the membrane fusion protein. This model selects a subfamily closely related to HlyD; it is defined narrowly and excludes, for example, colicin V secretion protein CvaA and multidrug efflux proteins. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 130902 [Multi-domain] Cd Length: 423 Bit Score: 68.88 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 219 VESTTSFSGRFRPGDVITLVSPFESTVVAR-HVEYGERVDEGDLLLELDST-------EIDIRYRRARSDLA--DAESEL 288
Cdd:TIGR01843 27 LDVVATATGKVVPSGNVKVVQHLEGGIVREiLVREGDRVKAGQVLVELDATdveadaaELESQVLRLEAEVArlRAEADS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 289 EDL----------------EDWEQGREMASSRRSLRQAERNLSNDQ--------------------------RELDDVEH 326
Cdd:TIGR01843 107 QAAiefpddllsaedpavpELIKGQQSLFESRKSTLRAQLELILAQikqleaelaglqaqlqalrqqlevisEELEARRK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 327 LFERGIVP-------ERELRAARERVEESRVRVEAAREDLAETSRQGGE----------RAIARARVEVENARAEYEQVQ 389
Cdd:TIGR01843 187 LKEKGLVSrlellelERERAEAQGELGRLEAELEVLKRQIDELQLERQQieqtfreevlEELTEAQARLAELRERLNKAR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 390 RQRDGARVYAPVDGVVlaplgedrddgERVE---AGGRVSSGAALLAVGDLS-SLEIEGTVDELDIHDVQAGQSARVNV- 464
Cdd:TIGR01843 267 DRLQRLIIRSPVDGTV-----------QSLKvhtVGGVVQPGETLMEIVPEDdPLEIEAKLSPKDIGFVHVGQPAEIKFs 335
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 648489684 465 ----VRGGGdpMPARVSYVSSQAQEGSGRGLPSFRLVVRIDD---LDDQDLERIRVGMSASVDVIT 523
Cdd:TIGR01843 336 afpyRRYGI--LNGKVKSISPDTFTDERGGGPYYRVRISIDQntlGIGPKGLELSPGMPVTADIKT 399
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
10-173 |
2.72e-11 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 65.75 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 10 QQILDSMADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFIGEEGYAAFVDALFEAVysgvmqpDQMVSISVG 89
Cdd:COG5000 93 ETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLREALERGW-------QEEIELTRD 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 90 GhVRSLKLTTSYLaprqagGERAVLAVFTDVTDLEQARQAE------QSLSDEL------------RGKHKELQDAFLEI 151
Cdd:COG5000 166 G-RRTLLVRASPL------RDDGYVIVFDDITELLRAERLAawgelaRRIAHEIknpltpiqlsaeRLRRKLADKLEEDR 238
|
170 180
....*....|....*....|..
gi 648489684 152 EANSEALQQAYRRSGRMRLMMT 173
Cdd:COG5000 239 EDLERALDTIIRQVDRLKRIVD 260
|
|
| PRK15136 |
PRK15136 |
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA; |
232-531 |
9.53e-11 |
|
multidrug efflux MFS transporter periplasmic adaptor subunit EmrA;
Pssm-ID: 185090 [Multi-domain] Cd Length: 390 Bit Score: 63.94 E-value: 9.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 232 GDVITLVSPFESTVVARHVEYGERVDEGDLLLELDSTEIDIRYRRARSDLADAESELEDLedweqgreMASSRR-----S 306
Cdd:PRK15136 59 GNQVQIMSQVSGSVTKVWADNTDFVKEGDVLVTLDPTDAEQAFEKAKTALANSVRQTHQL--------MINSKQyqaniE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 307 LRQAErnLSNDQRELDDVEHLFERGIVPERELRAARERVEESRVRVEAAREDLAetSRQG--------GERAIARARVEV 378
Cdd:PRK15136 131 LQKTA--LAQAQSDLNRRVPLGNANLIGREELQHARDAVASAQAQLDVAIQQYN--ANQAmilntpleDQPAVQQAATEV 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 379 ENAraeYEQVQRqrdgARVYAPVDGVVlaplgedrddGER-VEAGGRVSSGAALLAVGDLSSLEIEGTVDELDIHDVQAG 457
Cdd:PRK15136 207 RNA---WLALQR----TKIVSPMTGYV----------SRRsVQVGAQISPTTPLMAVVPATNLWVDANFKETQLANMRIG 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 458 QSARV-------NVVRGG---GDPMPARVSYVSSQAQEGSGRGLPSF-RLVVRIdDLDDQDLER--IRVGMSASVDVITq 524
Cdd:PRK15136 270 QPATItsdiygdDVVYTGkvvGLDMGTGSAFSLLPAQNATGNWIKVVqRLPVRI-ELDAKQLAQhpLRIGLSTLVTVDT- 347
|
....*..
gi 648489684 525 QDSDAVV 531
Cdd:PRK15136 348 ANRDGQV 354
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
11-129 |
1.12e-10 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 59.23 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 11 QILDSMADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFigEEGYAAFVDALFEAVYSGVMQPDQM--VSISV 88
Cdd:TIGR00229 7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELI--PEEDREEVRERIERRLEGEPEPVSEerRVRRK 84
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 648489684 89 GGHVRSLKLTTSYLapRQAGGERAVLAVFTDVTDLEQARQA 129
Cdd:TIGR00229 85 DGSEIWVEVSVSPI--RTNGGELGVVGIVRDITERKEAEEA 123
|
|
| PRK03598 |
PRK03598 |
putative efflux pump membrane fusion protein; Provisional |
249-462 |
7.87e-10 |
|
putative efflux pump membrane fusion protein; Provisional
Pssm-ID: 235136 [Multi-domain] Cd Length: 331 Bit Score: 60.75 E-value: 7.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 249 HVEYGERVDEGDLLLELDSTEIDIRYRRARSDLADAESELEDLEDWEQGREMASSRRSLRQAERNLSNDQRELDDVEHLF 328
Cdd:PRK03598 58 AVDEGDAVKAGQVLGELDAAPYENALMQAKANVSVAQAQLDLMLAGYRDEEIAQARAAVKQAQAAYDYAQNFYNRQQGLW 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 329 ERGIVPERELRAARERVEESRVRVEAAREDLAETSRQGGERAIARARVEVENARAEYEQVQRQRDGARVYAPVDGVVLAp 408
Cdd:PRK03598 138 KSRTISANDLENARSSRDQAQATLKSAQDKLSQYREGNRPQDIAQAKASLAQAQAALAQAELNLQDTELIAPSDGTILT- 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 648489684 409 lgedrddgERVEAGGRVSSGAALLAVGDLSSLEIEGTVDELDIHDVQAGQSARV 462
Cdd:PRK03598 217 --------RAVEPGTMLNAGSTVFTLSLTRPVWVRAYVDERNLGQAQPGRKVLL 262
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
10-120 |
9.12e-10 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 56.27 E-value: 9.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 10 QQILDSMADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFIgEEGYAAFVDALFEAVYSGvmQPDQMVSISVG 89
Cdd:pfam00989 4 RAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIP-EEDDAEVAELLRQALLQG--EESRGFEVSFR 80
|
90 100 110
....*....|....*....|....*....|....*
gi 648489684 90 ---GHVRSLKLTTSYLapRQAGGE-RAVLAVFTDV 120
Cdd:pfam00989 81 vpdGRPRHVEVRASPV--RDAGGEiLGFLGVLRDI 113
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
233-521 |
2.80e-09 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 58.88 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 233 DVITLVSPFESTVVARHVEYGERVDEGDLLLELDSTEIDIRYRRARSDLADAESELEDledweQGREM-------ASSRR 305
Cdd:PRK10476 47 DVVHVASEVGGRIVELAVTENQAVKKGDLLFRIDPRPYELTVAQAQADLALADAQIMT-----TQRSVdaersnaASANE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 306 SLRQAERNLSNDQRELDDVEHLFERGIVPERELRAARERVEESRVRVEAARE-DLAETSRQGGERAIARARVEVENARAe 384
Cdd:PRK10476 122 QVERARANAKLATRTLERLEPLLAKGYVSAQQVDQARTAQRDAEVSLNQALLqAQAAAAAVGGVDALVAQRAAREAALA- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 385 yeQVQRQRDGARVYAPVDGVVLaplgedrddGERVEAGGRVSSGAALLAVGDLSSLEIEGTVDELDIHDVQAGQSARVNV 464
Cdd:PRK10476 201 --IAELHLEDTTVRAPFDGRVV---------GLKVSVGEFAAPMQPIFTLIDTDHWYAIANFRETDLKNIRVGDCATVYS 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648489684 465 VRGGGDPMPARVSYVSSQAQEGSG----RGLP-----------SFRLVVRIdDLDDQDLERIRVGMSASVDV 521
Cdd:PRK10476 270 MIDRGRPFEGKVDSIGWGVLPDDGgnvpRGLPyvprsinwvrvAQRFPVRI-MLDKPDPELFRIGASAVVEL 340
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
10-129 |
6.08e-09 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 57.34 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 10 QQILDSMADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFIGEEgyAAFVDALFEAVYSGVMQPDQMVSISVG 89
Cdd:COG2202 140 RLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPED--RERLLELLRRLLEGGRESYELELRLKD 217
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 648489684 90 GHVRSLKLTTSYLAPRQAGGERAVLAVFTDVTDLEQARQA 129
Cdd:COG2202 218 GDGRWVWVEASAVPLRDGGEVIGVLGIVRDITERKRAEEA 257
|
|
| PRK11556 |
PRK11556 |
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit; |
197-585 |
6.10e-09 |
|
MdtA/MuxA family multidrug efflux RND transporter periplasmic adaptor subunit;
Pssm-ID: 183194 [Multi-domain] Cd Length: 415 Bit Score: 58.26 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 197 GASDAPVVDATqpgafeVQSRAVESTTSFSGRFRPGDVITLVSPFESTVVARHVEYGERVDEGDLLLELDSteidiryRR 276
Cdd:PRK11556 56 SGPLAPVQAAT------ATEQAVPRYLTGLGTVTAANTVTVRSRVDGQLMALHFQEGQQVKAGDLLAEIDP-------RP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 277 ARSDLADAESELedledweqgremASSRRSLRQAERNLSNDQRelddvehLFERGIVPERELRAARERVEESRVRVEAar 356
Cdd:PRK11556 123 FKVALAQAQGQL------------AKDQATLANARRDLARYQQ-------LAKTNLVSRQELDAQQALVSETEGTIKA-- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 357 edlaetsrqgGERAIARARVevenaraeyeqvqrQRDGARVYAPVDGVVlaplgedrddG-ERVEAGGRVSSGAA--LLA 433
Cdd:PRK11556 182 ----------DEASVASAQL--------------QLDYSRITAPISGRV----------GlKQVDVGNQISSGDTtgIVV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 434 VGDLSSLEIEGTVDELDIHDVQAGQSArvnvvrggGDPMPARVSYVSSQAQEGSGRGLP----------SFRLVVRIDDL 503
Cdd:PRK11556 228 ITQTHPIDLVFTLPESDIATVVQAQKA--------GKPLVVEAWDRTNSKKLSEGTLLSldnqidattgTIKLKARFNNQ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 504 DDQDLERIRVGMSASVDviTQQdsDAVVVPHAYL--GGSGSERWVLRQTSNGSERIaVELGRSRYDGVQVRSGVEPGDRL 581
Cdd:PRK11556 300 DDALFPNQFVNARMLVD--TLQ--NAVVIPTAALqmGNEGHFVWVLNDENKVSKHL-VTPGIQDSQKVVISAGLSAGDRV 374
|
....
gi 648489684 582 LPPG 585
Cdd:PRK11556 375 VTDG 378
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
10-60 |
1.24e-08 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 51.63 E-value: 1.24e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 648489684 10 QQILDSMADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFIGEE 60
Cdd:smart00091 4 RAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPED 54
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
10-138 |
3.78e-08 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 54.65 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 10 QQILDSMADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFIGEEGyAAFVDALFEAVYSGVMQPDQMVSISVG 89
Cdd:COG2202 14 RALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDD-DEFLELLRAALAGGGVWRGELRNRRKD 92
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 648489684 90 GHVRSLKLTTSYLaPRQAGGERAVLAVFTDVTDLEQARQAEQSLSDELR 138
Cdd:COG2202 93 GSLFWVELSISPV-RDEDGEITGFVGIARDITERKRAEEALRESEERLR 140
|
|
| HlyD_3 |
pfam13437 |
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator ... |
396-514 |
5.18e-08 |
|
HlyD family secretion protein; This is a family of largely bacterial haemolysin translocator HlyD proteins.
Pssm-ID: 433206 [Multi-domain] Cd Length: 104 Bit Score: 51.21 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 396 RVYAPVDGVVLaplgeDRDdgerVEAGGRVSSGAALLAVGDLSSLEIEGTVDELDIHDVQAGQSARVNVVRGGGDPMPAR 475
Cdd:pfam13437 1 TIRAPVDGVVA-----ELN----VEEGQVVQAGDPLATIVPPDRLLVEAFVPAADLGSLKKGQKVTLKLDPGSDYTLEGK 71
|
90 100 110
....*....|....*....|....*....|....*....
gi 648489684 476 VSYVSSQAQEGSGRglpsFRLVVRIDDLDDQDLerIRVG 514
Cdd:pfam13437 72 VVRISPTVDPDTGV----IPVRVSIENPKTPIP--LLPG 104
|
|
| HlyD_D23 |
pfam16576 |
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and ... |
397-517 |
1.19e-07 |
|
Barrel-sandwich domain of CusB or HlyD membrane-fusion; HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.
Pssm-ID: 435440 [Multi-domain] Cd Length: 214 Bit Score: 52.51 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 397 VYAPVDGVVLaplgedrddgER-VEAGGRVSSGAALLAVGDLSSLEIEGTVDELDIHDVQAGQSARVNVVRGGGDPMPAR 475
Cdd:pfam16576 111 VYAPISGVVT----------ELnVREGMYVQPGDTLFTIADLSTVWVEADVPEQDLALVKVGQPAEVTLPALPGKTFEGK 180
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 648489684 476 VSYVSSQAQegsgrglPSFR-LVVRIdDLDDQDLeRIRVGMSA 517
Cdd:pfam16576 181 VDYIYPTLD-------PKTRtVRVRI-ELPNPDG-RLKPGMFA 214
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
13-125 |
1.01e-06 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 47.41 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 13 LDSMADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFiGEEGYAAFVDALFEAVYSGVMQPDQMVSISVGGHV 92
Cdd:pfam08448 1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELL-PPEDAARLERALRRALEGEEPIDFLEELLLNGEER 79
|
90 100 110
....*....|....*....|....*....|....
gi 648489684 93 RslkLTTSYLAPRQAGGE-RAVLAVFTDVTDLEQ 125
Cdd:pfam08448 80 H---YELRLTPLRDPDGEvIGVLVISRDITERRR 110
|
|
| CitA |
COG3290 |
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
12-159 |
7.98e-06 |
|
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];
Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 48.31 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 12 ILDSMADGVLVVDASGAITTLNPAGAAILGLradEAEGRSLAEVFigeegyaafvdalfeavYSGVMQPDQMVSISVGGH 91
Cdd:COG3290 89 VLESIREGVIAVDRDGRITLINDAARRLLGL---DAIGRPIDEVL-----------------AEVLETGERDEEILLNGR 148
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648489684 92 VrslkLTTSYLAPRQAGGERAVLAVFTDVTDLEQARQ---AEQSLSDELRG-KH---KELQ--DAFLEIEANSEALQ 159
Cdd:COG3290 149 V----LVVNRVPIRDDGRVVGAVATFRDRTELERLEEeleGVKELAEALRAqRHdfrNHLHtiSGLLQLGEYDEALE 221
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
11-125 |
1.01e-05 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 48.43 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 11 QILDSMADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFIGEEGYaaFVDALF-EAVYSGVMQPDQMVSISVG 89
Cdd:COG5809 145 LIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQE--NVAAFIsQLLKDGGIAQGEVRFWTKD 222
|
90 100 110
....*....|....*....|....*....|....*.
gi 648489684 90 GHVRslKLTTSYLAPRQAGGERAVLAVFTDVTDLEQ 125
Cdd:COG5809 223 GRWR--LLEASGAPIKKNGEVDGIVIIFRDITERKK 256
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
16-120 |
1.45e-05 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 44.16 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 16 MADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFIGEEgYAAFVDALFEAVYSGVMQPDQMVSISVGGHVRSL 95
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPED-REELRERLENLLSGGEPVTLEVRLRRKDGSVIWV 79
|
90 100
....*....|....*....|....*
gi 648489684 96 kLTTSYLAPRQAGGERAVLAVFTDV 120
Cdd:cd00130 80 -LVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
10-60 |
2.58e-05 |
|
PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463802 [Multi-domain] Cd Length: 65 Bit Score: 42.15 E-value: 2.58e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 648489684 10 QQILDSMADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFIGEE 60
Cdd:pfam13188 4 RALFESSPDGILVLDEGGRIIYVNPAALELLGYELLGELLGELLDLLDPLL 54
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
269-449 |
2.60e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 269 EIDIRYRRARSDLADAESELEDLEDWEQGREMAssrRSLRQAERNLSNDQRELDDVEHLFERGIVPERELRAARERVEES 348
Cdd:COG4717 99 ELEEELEELEAELEELREELEKLEKLLQLLPLY---QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAEL 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 349 RVRVEAAREDLAETSRQGGERAI---ARARVEVENARAEYEQVQRQRDGARvyAPVDGvvLAPLGEDRDDGERVEAGGRV 425
Cdd:COG4717 176 QEELEELLEQLSLATEEELQDLAeelEELQQRLAELEEELEEAQEELEELE--EELEQ--LENELEAAALEERLKEARLL 251
|
170 180
....*....|....*....|....
gi 648489684 426 SSGAALLAVGDLSSLEIEGTVDEL 449
Cdd:COG4717 252 LLIAAALLALLGLGGSLLSLILTI 275
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
260-393 |
3.36e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 260 DLLLELDSTEIDIR--------YRRARSDLADAESELEDL----EDWEQGREMASSRRSLRQAERNLS--NDQRELDDVE 325
Cdd:COG4913 215 EYMLEEPDTFEAADalvehfddLERAHEALEDAREQIELLepirELAERYAAARERLAELEYLRAALRlwFAQRRLELLE 294
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 648489684 326 HLFERGivpERELRAARERVEESRVRVEAAREDLAETSRQ----GGERaIARARVEVENARAEYEQVQRQRD 393
Cdd:COG4913 295 AELEEL---RAELARLEAELERLEARLDALREELDELEAQirgnGGDR-LEQLEREIERLERELEERERRRA 362
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
260-396 |
1.86e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 260 DLLLELDstEIDIRYRRARSDLADAESELEDLEDweqgrEMASSRRSLRQAERNLSNDQRELDDVEHlfergivperELR 339
Cdd:COG1579 7 RALLDLQ--ELDSELDRLEHRLKELPAELAELED-----ELAALEARLEAAKTELEDLEKEIKRLEL----------EIE 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 648489684 340 AARERVEESRVRVEAAR-----------EDLAETSRQGGERAIARARVEVENARAEYEQVQRQRDGAR 396
Cdd:COG1579 70 EVEARIKKYEEQLGNVRnnkeyealqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
273-393 |
5.55e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 5.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 273 RYRRARSDLADAESELEDLEDWEQgrEMASSRRSLRQAERNLSNDQRELDDVEHLfERGIVPERELRAARERVEESRVRV 352
Cdd:COG4717 72 ELKELEEELKEAEEKEEEYAELQE--ELEELEEELEELEAELEELREELEKLEKL-LQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 648489684 353 EAAREDLAETSRQggERAIARARVEVENARAEYEQVQRQRD 393
Cdd:COG4717 149 EELEERLEELREL--EEELEELEAELAELQEELEELLEQLS 187
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
263-390 |
7.88e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 263 LELDSTEIDIRYRRARSDLADAESELEDLED----WEQGREMASSRRSLRQAERNLSNDQRELDDVEhlfergiVPEREL 338
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQErreaLQRLAEYSWDEIDVASAEREIAELEAELERLD-------ASSDDL 687
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 648489684 339 RAARERVEESRVRVEAAREDLAETSRQGG--ERAIARARVEVENARAEYEQVQR 390
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGrlEKELEQAEEELDELQDRLEAAED 741
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
273-396 |
1.00e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 273 RYRRARSDLADAESELEDLEDWEQgremasSRRSLRQAERNLSNDQRELDDVEHLfERGIvpeRELRAARERVEESRVRV 352
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELD------ALQERREALQRLAEYSWDEIDVASA-EREI---AELEAELERLDASSDDL 687
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 648489684 353 EAAREDL--AETSRQGGERAIARARVEVENARAEYEQVQRQRDGAR 396
Cdd:COG4913 688 AALEEQLeeLEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
272-386 |
1.17e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 272 IRYRRARSDLADAESELEDLEDW--EQGREMASSRRSLRQAERNLSNDQRELDDVEH--LFERGIVPERELRAARERVEE 347
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEEldKAFEELAETEKRLEELRKELEELEKKYSEEEYeeLREEYLELSRELAGLRAELEE 684
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 648489684 348 SRVRVEAAREDLAETSRQGGERAIARARVEV-ENARAEYE 386
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEELEEREKAKKELEKlEKALERVE 724
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
261-396 |
1.43e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 261 LLLELDstEIDIRYRRARSDLADAESELEDLEDWEQGREMASSRRSLRQAERNLSNDQRELDDVEHLfERGIVPERELRA 340
Cdd:COG1196 230 LLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL-AELARLEQDIAR 306
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 648489684 341 ARERVEESRVRVEAAREDLAETSRQGGERA--IARARVEVENARAEYEQVQRQRDGAR 396
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEeeLEELEEELEEAEEELEEAEAELAEAE 364
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
250-418 |
1.79e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.10 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 250 VEYGERVDE--GDLLLELDSTEIDIRYRRARSDLADAESELED-LEDWEQGREMASSRR----SLRQAERNLSNDQRELD 322
Cdd:COG5185 274 AESSKRLNEnaNNLIKQFENTKEKIAEYTKSIDIKKATESLEEqLAAAEAEQELEESKRetetGIQNLTAEIEQGQESLT 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 323 DVEHL---FERGIVPERELRAARERVEESRVRVEAAREDL------AETSRQGGERAIARARVEVENaraEYEQVQRQRD 393
Cdd:COG5185 354 ENLEAikeEIENIVGEVELSKSSEELDSFKDTIESTKESLdeipqnQRGYAQEILATLEDTLKAADR---QIEELQRQIE 430
|
170 180
....*....|....*....|....*
gi 648489684 394 GARVYAPVDGVVLAPLGEDRDDGER 418
Cdd:COG5185 431 QATSSNEEVSKLLNELISELNKVMR 455
|
|
| Biotin_lipoyl_2 |
pfam13533 |
Biotin-lipoyl like; |
233-282 |
2.18e-03 |
|
Biotin-lipoyl like;
Pssm-ID: 433286 Cd Length: 50 Bit Score: 36.27 E-value: 2.18e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 648489684 233 DVITLVSPFESTVVARHVEYGERVDEGDLLLELDSTEIDIRYRRARSDLA 282
Cdd:pfam13533 1 PVVKIASPVSGKVVAVNVKEGQQVKKGDVLATLDSPELQLQLQQAEAQLA 50
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
262-396 |
2.39e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 262 LLELDSTEIDIRYRRARsdLADAESELEDLEdweqgremaSSRRSLRQAERNLSNDQRELDDVEHLFERGIVPERELRAA 341
Cdd:COG4913 653 LAEYSWDEIDVASAERE--IAELEAELERLD---------ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE 721
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 648489684 342 RERVEESRVRVEAAREDLAETSRQgGERAIARARVEVENARAEYEQVQRQRDGAR 396
Cdd:COG4913 722 LEQAEEELDELQDRLEAAEDLARL-ELRALLEERFAAALGDAVERELRENLEERI 775
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
270-393 |
2.88e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 270 IDIRYRRARSDLADAESELEDLEdweqgREMASSRRSLRQAERNLSNDQRELDDVEhlfergivpeRELRAARERVEESR 349
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLR-----EELEQAREELEQLEEELEQARSELEQLE----------EELEELNEQLQAAQ 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 648489684 350 VRVEAAREDLAETSRQggeraIARARVEVENARAEYEQVQRQRD 393
Cdd:COG4372 94 AELAQAQEELESLQEE-----AEELQEELEELQKERQDLEQQRK 132
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
254-434 |
3.77e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 3.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 254 ERVDEGDLLLELDSTEIDI--RYRRARSDLADAESELEDLEDWEQGREMASSRRSLRQAERNLSNDQRELDDVEHLFERG 331
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAeeELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 332 IVpERELRAARERVEESRVRVEAAREDLAE--TSRQGGERAIARARVEVENARAEYEQVQRQRDGARVYA---------P 400
Cdd:COG1196 439 EE-EEALEEAAEEEAELEEEEEALLELLAEllEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLegvkaalllA 517
|
170 180 190
....*....|....*....|....*....|....
gi 648489684 401 VDGVVLAPLGEDRDDGERVEAGGRVSSGAALLAV 434
Cdd:COG1196 518 GLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI 551
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
299-365 |
4.26e-03 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 39.64 E-value: 4.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 648489684 299 EMASSRRSLRQAERNLSNDQRELDDVEHLFERGIVPERELRAARERVEESRVRVEAAREDLAETSRQ 365
Cdd:COG1538 84 DLLAAQEQLALAEENLALAEELLELARARYEAGLASRLDVLQAEAQLAQARAQLAQAEAQLAQARNA 150
|
|
| glnL |
PRK11073 |
nitrogen regulation protein NR(II); |
8-103 |
4.75e-03 |
|
nitrogen regulation protein NR(II);
Pssm-ID: 182947 [Multi-domain] Cd Length: 348 Bit Score: 39.68 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 8 LSQQILDSMADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFigeeGYAAF-VDALFEAVYSGVMQPDQMVSI 86
Cdd:PRK11073 8 DAGQILNSLINSILLLDDDLAIHYANPAAQQLLAQSSRKLFGTPLPELL----SYFSLnIELMRESLQAGQGFTDNEVTL 83
|
90
....*....|....*..
gi 648489684 87 SVGGHVRSLKLTTSYLA 103
Cdd:PRK11073 84 VIDGRSHILSLTAQRLP 100
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
254-385 |
4.94e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 254 ERVDEGDLLLEldstEIDIRYRRARSDLADAESELEDLEdweqgREMASSRRSLRQAERNLSNDQRELDDVEHLFERGIV 333
Cdd:COG4913 678 ERLDASSDDLA----ALEEQLEELEAELEELEEELDELK-----GEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 648489684 334 PERELRAARERVEESRVRVeaaREDLAEtSRQGGERAIARARVEVENARAEY 385
Cdd:COG4913 749 ALLEERFAAALGDAVEREL---RENLEE-RIDALRARLNRAEEELERAMRAF 796
|
|
| MnmE |
COG0486 |
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal ... |
275-397 |
5.18e-03 |
|
tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying GTPase MnmE/TrmE is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 440253 [Multi-domain] Cd Length: 448 Bit Score: 39.66 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 275 RRA----RSDLADAESeLEDLEDweqgremASSRRSLRQAERNLSNDQRelddvehlfergivpeRELRAARERVEESRV 350
Cdd:COG0486 110 KRAflngKLDLTQAEA-VADLID-------AETEAAARQALRQLSGALS----------------RRIEELRERLLDLLA 165
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 648489684 351 RVEAA----REDLAETSRQGGERAIARARVEVENARAEYEQVQRQRDGARV 397
Cdd:COG0486 166 LIEAAidfpEEDVEFLDREELLERLEELREELEALLASARQGELLREGIKV 216
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
10-133 |
6.35e-03 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 39.19 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 10 QQILDSMADGVLVVDASGAITTLNPAGAAILGLRADEAEGRSLAEVFIGEEGYaaFVDALFEAVYSGVMQPDQMVSISVG 89
Cdd:COG5809 18 RSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEK--ELREILKLLKEGESRDELEFELRHK 95
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 648489684 90 -GHVRSLKLTTSYLApRQAGGERAVLAVFTDVTDL----EQARQAEQSL 133
Cdd:COG5809 96 nGKRLEFSSKLSPIF-DQNGDIEGMLAISRDITERkrmeEALRESEEKF 143
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
120-397 |
6.65e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.37 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 120 VTDLEQARQAEQSLSDELRGKHKELQDAFLEIEANSEAL--QQAYRRSGRMRLMMTAAVVAVFAGAGYWAIPNAALPEFG 197
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAG 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 198 AsdAPVVDATQPGAFEVQSRAVESTTSFSGRFRPGDVITLVSPFESTVVARHVEYGERVDEGDLLLELDSTEidiRYRRA 277
Cdd:COG4717 278 V--LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE---ELQEL 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 278 RSDLADAESEL------------------EDLEDWEQGREMASSRRSLRQAERNLSNDQRELDDVEHLFERGIVPER--- 336
Cdd:COG4717 353 LREAEELEEELqleeleqeiaallaeagvEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEElee 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648489684 337 ELRAARERVEESRVRVEAAREDLAETSRQ----GGERAIARARVEVENARAEYEQVQRQRDGARV 397
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAEleqlEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
251-392 |
7.62e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 39.28 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 251 EYGERVDEGDLLLElDSTEIDIRYRRARSDLADAESELEDLedweqGREMASSRRSLRqaernlsndqRELDDVEHLFER 330
Cdd:TIGR02169 358 EYAELKEELEDLRA-ELEEVDKEFAETRDELKDYREKLEKL-----KREINELKRELD----------RLQEELQRLSEE 421
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 648489684 331 GIVPERELRAARERVEESRVRVEAAREDLaETSRQGGERAIA---RARVEVENARAEYEQVQRQR 392
Cdd:TIGR02169 422 LADLNAAIAGIEAKINELEEEKEDKALEI-KKQEWKLEQLAAdlsKYEQELYDLKEEYDRVEKEL 485
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
242-394 |
8.02e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.25 E-value: 8.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 242 ESTVVARHVEYGERVDEGDLLL---ELDSTEIDIRYRRArSDLADAESELEDLEDweqGREMASSRRSLRqaeRNLSNDQ 318
Cdd:PRK02224 463 GSPHVETIEEDRERVEELEAELedlEEEVEEVEERLERA-EDLVEAEDRIERLEE---RREDLEELIAER---RETIEEK 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 648489684 319 REldDVEHLFERGIVPERELRAARERVEESRVRVEAAREDLAETSRQGGERAIARARVE--------VENARAEYEQVQR 390
Cdd:PRK02224 536 RE--RAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirtllaaIADAEDEIERLRE 613
|
....
gi 648489684 391 QRDG 394
Cdd:PRK02224 614 KREA 617
|
|
| |
